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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the reaction is initiated by blue light and proceeds through long-range energy transfer, single electron transfer and enzyme catalysis by a radical mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
mechanism of photoactivation
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
by molecular dynamics simulation and quantum mechanical calculations it is shown that indirect electron tunneling via the protein medium is as important as direct electron transfer from the donor (FADH-) to the acceptor (cyclobutane pyrimidine dimmer). At Met353 site busy electron tunneling traffic is observed.
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
results support the electron hopping mechanism by which electron transfer from W306 to the flavin is mediated in a three-step electron hopping process (W306 to W359 to W382 to FADH)
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
on top of the transient formation of tryptophan radicals during photoactivation, evidence is found for oxidation of a tyrosine residue by a tryptophan radical. The tyrosine radical thus formed is reduced by an extrinsic reductant, suggesting that in this case the terminal intrinsic electron donor is tyrosine rather than tryptophan
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism, detailed overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
upon absorption of a visible photon, the photoexcited flavin radical FADH abstracts an electron from nearby W382. The tryptophanyl radical W382 thus formed abstracts an electron from the nearby middle tryptophan, W359. W359 radical abstracts an electron from W306. As the second and third steps are faster than the first one, the intermediate states are not populated in wild-type photolyase to any significant extent and escape spectroscopic detection. The described forward electron transfer steps between the tryptophans are in competition with back electron transfer from FADH- to the respective tryptophanyl cation radical, so that the quantum yield of formation of the terminal W306 radical is only 20%. W306 radical releases a proton to the aqueous phase in 200 ns. The resulting neutral radical W306 radical can be reduced by extrinsic reductants, leaving a photolyase that contains FADH as required for photorepair of DNA
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
using a transient absorption setup, cyclobutane thymine dimer repair in the main UV absorption band of intact thymine at 266 nm is monitored. Flavin transitions that overlay DNA-based absorption changes at 266 nm are monitored independently in the visible and subtracted to obtain the true repair kinetics. Restoration of intact thymine show a short lag and a biexponential rise with time constants of 0.2 and 1.5 ns. The two time constants are assigned to splitting of the intradimer bonds (creating one intact thymine and one thymine anion radical T-) and electron return from T- to the FAD cofactor with recovery of the second thymine, respectively
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
cyclic electron-transfer radical mechanism with two fundamental processes, electron-tunneling pathways and cyclobutane ring splitting, the cyclobutane pyrimidine dimer splits in two sequential steps within 90 ps and the electron tunnels between the cofactor and substrate through a remarkable route with an intervening adenine, dynamics and mechanism of cyclobutane pyrimidine dimer repair by DNA photolyase, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
substrate/cofactor binding and reaction mechanism, catalytic active site Met397, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the DNA repair enzyme recognizes a solvent-exposed cyclobutadipyrimidine as part of its damage recognition mechanism
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
dynamics and mechanism of CPD repair by photolyase, detailed overview. In contrast to the computational reaction model the thymine dimer splits by a sequential pathway
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
molecular mechanism of the electron transfer, overview. The electronic coupling matrix element is 36/cm from the donor (FADH-) to the acceptor (CPD) by Mulliken-Hush (GMH) method and the bridge green function (GF) methods, and the estimated electron transfer time is 386 ps. Molecular dynamics simulations and ab initio molecular orbital calculations, and exploration of the electron tunneling pathway for 20 different structures during the MD trajectory, QM/MM calculation. The electron transfer route via Asn349 is the dominant pathway among the five major routes via (adenine/Asn349), (adenine/Glu283), (adenine/Glu283/Asn349/Met353), (Met353/Asn349), and (Asn349), indicating that Asn349 is an essential amino acid residue in the electron transfer reaction
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
radical mechanism through a cyclic redox reaction. Photolyase binds DNA containing a CPD because the thymine dimer distorts the backbone of the DNA. Upon binding to damaged DNA, through ionic interactions between the positively charged groove on the photolyase surface and negatively charged DNA phosphodiester backbone the enzyme pulls the thymine dimer out from within the helix and into the core of the enzyme so that the thymine dimer is within Van der Waals contact with FADH-. It makes a very staple complex, and nothing happens until folate absorbs a photon and transfers the excitation energy to the flavin cofactor. The excited-state flavin, FADH- radical, repairs the thymine dimer by a cyclic redox reaction, and then the enzyme dissociates from the DNA to go on in search of other damage sites to carry out the repair reactions again
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview. Proposed intraprotein electron transfer from W306 to FADH radical is not a part of the normal photolyase photocycle in vivo
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA. The initial step involves photoinduced electron transfer from FADH- radical to the CPD. The adenine (Ade) moiety is nearly stacked with the flavin ring, an unusual conformation compared to other FAD-dependent proteins
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
molecular mechanism of the electron transfer, overview. The electronic coupling matrix element is 36/cm from the donor (FADH-) to the acceptor (CPD) by Mulliken-Hush (GMH) method and the bridge green function (GF) methods, and the estimated electron transfer time is 386 ps. Molecular dynamics simulations and ab initio molecular orbital calculations, and exploration of the electron tunneling pathway for 20 different structures during the MD trajectory, QM/MM calculation. The electron transfer route via Asn349 is the dominant pathway among the five major routes via (adenine/Asn349), (adenine/Glu283), (adenine/Glu283/Asn349/Met353), (Met353/Asn349), and (Asn349), indicating that Asn349 is an essential amino acid residue in the electron transfer reaction
-
-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
photo-induced intramolecular electron transfer in photolyases and initial electron-transfer bifurcation in repair complexes. Seven electron-transfer reactions in 10 elementary steps in all classes of CPD photolyases. Unified electron-transfer pathway through a conserved structural configuration that bifurcates to favor direct tunneling in prokaryotes and a two step hopping mechanism in eukaryotes. Complete photocycles of CPD repair by class I and class II PLs, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanism, detailed overview
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-
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
reaction mechanisms of CPD DNA photolyase and cytochrome DASH, detailed overview
-
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
-
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
the repair of CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route mediated by the intervening adenine and a two-step hopping path bridged by the intermediate adenine from the cofactor to damaged DNA, through the conserved folded flavin at the active site. Repair photocycle of the PLs and development of a unified repair mechanism for all CPD PLs with the critical, bifurcating electron transfer pathways through the folded flavin cofactor in the conserved active site structure, overview
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cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA)
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adenosine 5'-(beta,gamma-imido)triphosphate
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Cry1
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?
cis,syn-cyclobutane pyrimidine dimer
2 pyrimidine residues
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substrate binding and substrate conformation by isothermal titration calorimetry, overview
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?
cis-syn cyclobutadipyrimidine dimer DNA
pyrimidine residues in DNA
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
cyclobutadipyrimidine in calf thymus DNA
2 pyrimidine residues in calf thymus DNA
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optimal activity at 400 nm wavelength, no activity at 300 nm, 500 nm and in the dark
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
cyclobutadipyrimidine in DNA
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
cyclobutadipyrimidine in minichromosomes
2 pyrimidine residues in minichromosomes
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removes cyclobutane pyrimidine dimers predominantly from the ARS1 region
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?
cyclobutadipyrimidine in nucleosome DNA
2 pyrimidine residues in nucleosome DNA
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folding of DNA in nucleosomes efficiently protects DNA from being repaired
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?
cyclobutadipyrimidine in oligodeoxythymidylates
pyrimidine residues in oligodeoxythymidylates
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minimum size is about 9 residues
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?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
pyrimidine dimer in DNA
2 pyrimidine residues in DNA
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?
thymine dimers in AnCPDI and Atcry3 complexes
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additional information
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
enzyme AtCRY3 is specific for single-stranded DNA substrates
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
photolyases utilize near-ultraviolet blue light to specifically repair the major photoproducts of UV-induced damaged DNA. The enzyme specifically repairs CPD lesions
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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repair of a single CPD lesion within a double-stranded DNA molecule
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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various CPD substrates, T-T, T-U, U-T, U-U dimers
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the entire catalytic cycle is complete in 1.2 ns, and the enzyme repairs thymine dimer with a quantum yield of 0.9
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the substrate used in binding experiments, UV-p(dT)10 (denoted as ssDNA), is a single strand oligothymidylate with an average of a single CPD lesion randomly arranged on the 10mer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the substrate used in binding experiments, UV-p(dT)10 (denoted as ssDNA), is a single strand oligothymidylate with an average of a single CPD lesion randomly arranged on the 10mer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
the pyrimidine dimer is flipped out from the DNA helix into the central cavity, thereby coming within van der Waals contact distance of the FAD molecule. This central pocket is lined on one side with hydrophobic residues and with polar residues on the other, thus matching the asymmetric polarity of the thymidine dimer
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cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
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?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Xiphophorus maculatus Jp 163 B
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cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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repairs cyclobutylpyrimidine dimers by a light-driven electron transfer
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
two photolyases specific for photoreactivation of either cyclobutane pyrimidine dimers or pyrimidine (6-4)pyrimidones
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
AtCry3 repairs the dimer but only in ssDNA
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
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-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
enzyme uses light to repair cyclobutylpryrimidine dimers in DNA, local structure around the thymidine lesion changes dramatically upon binding to photolyase
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
upon binding of DNA, the enzyme flips the pyrimidine dimer out of the duplex into a hole that contains the catalytic cofactor. The cyclobutane ring is then split by a light-initiated electron transfer reaction
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
steady-state fluorescence measurements of single- and double-stranded oligonucleotides shows that the local region around the 5'-side of the cyclobutadipyrimidine lesion is more disrupted and destacked than the 3'-side in substrate-protein complexes
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
active genes are faster repaired than silenced genes
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
active genes are faster repaired than silenced genes
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
dimeric and pentameric oligothymidine substrates, repairs cyclobutylpyrimidine dimers via photoinduced electron transfer from a reduced flavin adenine dinucleotide cofactor to the bound cyclobutylpyrimidine dimer
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
repairs cyclobutylpyrimidine dimers by using visible light
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
specific for cyclobutane pyrimidine dimers
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
DNA repair activity
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
VcCry1 repairs the dimer but only in ssDNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
XlCry-DASH repairs the dimer but only in ssDNA
-
-
?
cyclobutadipyrimidine in DNA
?
compared to the wild-type the rate of cyclobutane pyrimidine dimer accumulation is increased in the uvr2-1 mutant but decreases in the CPD photolyase overexpressors. Under conditions without UV-B, overexpression of photolyase does not have any negative effect on growth
-
-
?
cyclobutadipyrimidine in DNA
?
-
-
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme binds to DNA containing pyrimidine dimers with high affinity and then breaks the cyclobutane ring joining the two pyrimidines of the dimer in a light-dependent reaction, 300-500 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
about 20times more pyrimidine dimers are bound to the yeast photolyase than to the Escherichia coli photolyase. Ratio between the enzyme's binding constant for pyrimidine dimers and its binding constant for nondamaged DNA is very similar for yeast and Escherichia coli photolyases
-
-
?
cyclobutadipyrimidine in DNA
?
-
photolyase binds tighter to substrate than cryptochrome 1, binding constant is slightly sensitive to oxidation state
-
-
?
cyclobutadipyrimidine in DNA
?
-
presence of a very rigid antenna binding site, a relatively rigid active site in CPD photolyase but with large local orientation flexibility
-
-
?
cyclobutadipyrimidine in DNA
?
-
-
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
about 20times more pyrimidine dimers are bound to the yeast photolyase than to the Escherichia coli photolyase. Ratio between the enzyme's binding constant for pyrimidine dimers and its binding constant for nondamaged DNA is very similar for yeast and Escherichia coli photolyases
-
-
?
cyclobutadipyrimidine in DNA
?
-
the larger N-terminal domain of primase carboxy-terminal domain (PriL-CTD) assists the smaller catalytic subunit PriS in the simultaneous binding of the two initial ribonucleotides and in promoting their Watson-Crick base pairing at the initiation site on the template DNA
-
-
?
cyclobutadipyrimidine in DNA
?
-
-
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
photolyase binds tighter to substrate than cryptochrome 1, binding constant is slightly sensitive to oxidation state
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
the enzyme repairs specifically cyclobutane pyrimidine dimers in UV-damaged single-stranded DNA, the enzyme catalyzes light-driven DNA repair like conventional photolyases but lacks an efficient flipping mechanism for interaction with cyclobutane pyrimidine dimer lesions within duplex DNA
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
the substrate is a modified thymidine 10-mer with a central T = T and all other bases, except the one at the 3' end, replaced by 5,6-dihydrothymine (5S:5R stereoisomer ratio 90:10)
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
DNA repair enzyme can absorb blue/ultraviolet A light as energy and split a pyrimidine dimer induced by ultraviolet radiation. PHR1 gene encodes a functional photolyase. The PHR1 transcripts are specifically enhanced by near-ultraviolet radiation (300-400 nm) and by sunlight
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
UV inactivated Haemophilus influenzae DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light with wavelengths around 400 nm is utilized for DNA repair by PHR
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
the unique configuration of the phosphodiester backbone in the strand containing the pyrimidine dimer, as well as the cyclobutane ring of the dimer itself are the important structural determinants of the substrate for recognition by photolyase
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
binds to DNA containing pyrimidine dimers in a light-independent step and repairs the pyrimidine dimer upon absorbing a photon in the 300-600 nm range
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
no activity towards (6-4)pyrimidine-cytosine products in DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
inactive on dimers in RNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
active on cis-syn-cyclobutylpyrimidine dimers in supercoiled DNA as in linear DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
catalyzes the repair of cyclobutadipyrimidine dimers in DNA under near-UV or blue light irradiation
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
Frog
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
the enzyme is one of the main factors determining UVB sensitivity in Oryza sativa. Cultivar Sasanishiki is resistant to the damaging effects of UVB while cultivar Norin 1 is less resistant. Amino acid position 126 is Arg in cultivar Norin 1 and Gln in cultivar Sasanishiki. The single amino acid alteration from Gln to Arg leads to a deficit of CPD photolyase activity
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
the enzyme preferentially repairs the non-transcribed strands of the URA3 and HIS3 genes in minichromosomes, repair of the non-transcribed strand is more quickly in the active gene than in the repressed gene indicating that transcription dependent disruption of chromatin facilitates repair of an active gene
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
UV inactivated Haemophilus influenzae DNA
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolet irradiation, 220-320 nm
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
catalyzes photorepair of thymine dimers on UV damaged DNA
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
DNA photolyase recognizes ultraviolet-damaged DNA and breaks improperly formed covalent bonds within the cyclobutane pyrimidine dimer by a light-activated electron transfer reaction between FAD and cyclobutane pyrimidine dimer
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
NMR study of repair mechanism of DNA photolyase by FAD-induced paramagnetic relaxation enhancement
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
-
-
-
-
?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
-
-
-
-
?
cyclobutadipyrimidine in RNA
2 pyrimidine residues in RNA
-
-
-
-
?
cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
-
optimal activity at 400 nm wavelength, no activity at 300 nm, 500 nm and in the dark
-
?
cyclobutadipyrimidine in salmon sperm DNA
2 pyrimidine residues in salmon sperm DNA
-
high activity
-
?
cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
-
fast repair of the non-transcribed strand and slow repair of the transcribed strand
-
?
cyclobutadipyrimidine in yeast urea3 gene
2 pyrimidine residues in yeast urea3 gene
-
fast repair of the non-transcribed strand and slow repair of the transcribed strand
-
?
thymine dimers in AnCPDI and Atcry3 complexes
?
the conserved MmCPDII tryptophans W305 and W421 form the L-shaped walling of the active site that clamps the CPD lesion together with the side chain of the conserved M379. Upon repair the 5'-thymine base is expected to remain in place upon breakage of the C5-C5 and C6-C6 bonds by maintaining the p-stacking interactions with the indole moiety of W305, whereas the 3'-thymine dissociates by ca. 1 A away towards the thioether group of M379
-
-
?
thymine dimers in AnCPDI and Atcry3 complexes
?
-
the conserved MmCPDII tryptophans W305 and W421 form the L-shaped walling of the active site that clamps the CPD lesion together with the side chain of the conserved M379. Upon repair the 5'-thymine base is expected to remain in place upon breakage of the C5-C5 and C6-C6 bonds by maintaining the p-stacking interactions with the indole moiety of W305, whereas the 3'-thymine dissociates by ca. 1 A away towards the thioether group of M379
-
-
?
additional information
?
-
environmental stress enzyme
-
-
?
additional information
?
-
-
environmental stress enzyme
-
-
?
additional information
?
-
light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
-
?
additional information
?
-
-
light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
-
?
additional information
?
-
-
pre-inoculation UV-C (254 nm) treatment of normally susceptible Arabidopsis thaliana accessions induces prolonged, dose-dependent resistance to virulent isolates of the phytopathogenic oomycete Hyaloperonospora parasitica with cyclobutane pyrimidine dimers and (6-4) photoproducts playing a key role in this response
-
-
?
additional information
?
-
-
CPD-photolyase is a DNA repair protein, the electron-transport chain of Cry1 involves a Tyr residue as initial electron donor. For Cry3, weak but unspecific DNA binding, for Cry1, DNA binding cannot be detected. Cry2, whose surface largely resembles that of Cry1, does bind to DNA. Cry3 does repair cyclobutane-pyrimidine-dimers when the lesion is located in a preflipped out state such as in bulges of dsDNA. DASH cryptochromes are single-strand-specific CPD-photolyases
-
-
?
additional information
?
-
-
CryA can repair DNA upon exposure to UVA light similar to other photolyase proteins, CryA represses sexual development under UVA350-370 nm light and exhibits a regulatory function during light-dependent development and DNA repair activity, in the wild type strain mechanisms such as excision repair mask the DNA photolyase activity of CryA
-
-
?
additional information
?
-
the enzyme has blue light photoreceptor activity and CPD photolyase activity. Signaling might be mediated by the PHR besides its effects on the C-terminal extension, conformational changes in cryptochromes upon illumination, overview
-
-
?
additional information
?
-
-
the enzyme has blue light photoreceptor activity and CPD photolyase activity. Signaling might be mediated by the PHR besides its effects on the C-terminal extension, conformational changes in cryptochromes upon illumination, overview
-
-
?
additional information
?
-
conformational changes in the PHR, infrared spectral analysis and isotope labeling, overview
-
-
?
additional information
?
-
-
conformational changes in the PHR, infrared spectral analysis and isotope labeling, overview
-
-
?
additional information
?
-
-
CPD-photolyase binds 8-hydroxy-7,8-didemethyl-5-deazariboflavin which is an antenna chromophore present in various photolyases
-
-
?
additional information
?
-
-
PHR1 and PHR2 are able to bind the CLOCK protein, a transcription activator controlling the molecular circadian clock. But only for PHR2, the physical interaction with CLOCK represses CLOCK/BMAL1-driven transcription, binding of photolyase per se is not sufficient to inhibit the CLOCK/BMAL1 heterodimer
-
-
?
additional information
?
-
CpPL is fully competent to bind and base flip CPDs, and to repair them when exposed to blue light. rCpPL recognizes and flips out a CPD into its active site, base flipping of the CPD by photolyase is accompanied by a large distortion of the local structure of the DNA duplex around the lesion, including the loss of DNA base stacking. 2-Ap base-flipping assay, overview. Thermodynamically, the apparent lack of rigidity of the chains forming the active site would impart a high degree of conformational entropy to the active site of CpPL
-
-
?
additional information
?
-
CpPL is fully competent to bind and base flip CPDs, and to repair them when exposed to blue light. rCpPL recognizes and flips out a CPD into its active site, base flipping of the CPD by photolyase is accompanied by a large distortion of the local structure of the DNA duplex around the lesion, including the loss of DNA base stacking. 2-Ap base-flipping assay, overview. Thermodynamically, the apparent lack of rigidity of the chains forming the active site would impart a high degree of conformational entropy to the active site of CpPL
-
-
?
additional information
?
-
-
CPD photolyase, which rapidly repairs CPDs, is essential for plant survival under sunlight containing UVB
-
-
?
additional information
?
-
comparison of repair activity of the photolyase in the wild-type strain PGEX-4T-1-DsPHR2 and the mutant strain PGEX-4T-1-DsPHR2-Q336H in vitro and in vitro and under different salt concentrations, overview. The mutant shows reduced repair activity compared to wild-type, and the survival rate declines rapidly as salinity increased in the mutant Q336H, while in the wild-type strain, there is no change in the survival rate
-
-
?
additional information
?
-
-
major pathway to remove UV-induced DNA lesions from the genome
-
?
additional information
?
-
-
photoreduction by intraprotein electron transfer is not part of the photolyase photocycle under physiological conditions
-
-
?
additional information
?
-
-
4-amino-6-methyl-8-(2'-deoxy-beta-D-ribofuranosyl)-7(8H)-pteridone (6MAP) is a fluorescent adenine analogue that demonstrates high sensitivity to base-stacking interactions in duplex DNA. 6MAP is a sensitive probe of cyclobutylpyrimidine dimers base flipping by photolyase and does does not interfere with the repair of the substrate. It is shown that 6MAP/cyclobutylpyrimidine dimers duplexes are true substrates of photolyase
-
-
?
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
?
additional information
?
-
-
a novel substrate (a modified thymidine 10-mer with a central cyclobutane pyrimidine dimer and all bases, except the one at the 3' end, replaced by 5,6-dihydrothymine) is repaired with an efficiency very similar to that of the conventional substrates (a 10-mer of unmodified thymidines containing a central cyclobutane pyrimidine dimer and an acetone-sensitized thymidine 18-mer containing in average six randomly distributed cyclobutane pyrimidine dimers per strand). Significantly lower repair quantum yield for the holoenzyme compared to its apo form due to an additional process, i.e., excitation energy transfer from the antenna cofactor to the reduced flavin
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-
?
additional information
?
-
DNA repair protein
-
-
?
additional information
?
-
-
electrostatic interactions and protonation are affected by the oxidation state of the required FAD cofactor and substrate conformation
-
-
?
additional information
?
-
-
the enzyme shows light-induced reduction of FAD, and photorepair involves the transfer of an electron from the photoexcited reduced FAD to the damaged DNA for cleaving the dimers to maintain the DNA's integrity, substrate specificity, overview
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-
?
additional information
?
-
anaerobic repair assay in argon atmosphere
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-
?
additional information
?
-
detailed repair dynamics of damaged DNA by photolyases and a biomimetic system through resolving all elementary steps on the ultrafast timescales, including multiple intermolecular electron- and proton-transfer reactions and bond-breaking and -making processes
-
-
?
additional information
?
-
direct measurements of photolyase binding to cyclobutane pyrimidine dimers (CPD)-containing undecamer DNA that has been labeled with a fluorophore, photolyase csCPD-DNA binding kinetics detected by fluorescence spectroscopy, overview. Preparation and purification of csCPD-containing oligonucleotides. Photolyase finds its target through a three-dimensional diffusion-controlled search. Photolyase may not recognize an intrahelical CPD but only an extrahelical CPD
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-
?
additional information
?
-
-
direct measurements of photolyase binding to cyclobutane pyrimidine dimers (CPD)-containing undecamer DNA that has been labeled with a fluorophore, photolyase csCPD-DNA binding kinetics detected by fluorescence spectroscopy, overview. Preparation and purification of csCPD-containing oligonucleotides. Photolyase finds its target through a three-dimensional diffusion-controlled search. Photolyase may not recognize an intrahelical CPD but only an extrahelical CPD
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-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
photochemistry of wild-type and N378D mutant DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy, overview
-
-
?
additional information
?
-
-
photochemistry of wild-type and N378D mutant DNA photolyase with oxidized FAD cofactor studied by transient absorption spectroscopy, overview
-
-
?
additional information
?
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
-
Cry2 protein binds to ssDNA with high affinity
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-
?
additional information
?
-
-
the class II enzyme lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA, in contrast to class I enzymes. The lesion-binding mode differs from other photolyases by a larger DNA binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
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-
?
additional information
?
-
the class II enzyme lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA, in contrast to class I enzymes. The lesion-binding mode differs from other photolyases by a larger DNA binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
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-
?
additional information
?
-
enzyme-substrate complex structure of class II PL from Methanosarcina mazei (MmPL)
-
-
?
additional information
?
-
enzyme-substrate complex structure of class II PL from Methanosarcina mazei (MmPL)
-
-
?
additional information
?
-
-
the class II enzyme lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA, in contrast to class I enzymes. The lesion-binding mode differs from other photolyases by a larger DNA binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
-
-
?
additional information
?
-
PhrB does not function as a photolyase
-
-
?
additional information
?
-
-
PhrB does not function as a photolyase
-
-
?
additional information
?
-
PhrB does not function as a photolyase
-
-
?
additional information
?
-
the native rice CPD photolyase is phosphorylated, whereas the Escherichia coli-expressed rice CPD photolyase is not
-
-
?
additional information
?
-
-
expression in transgenic mice leads to superior survival, reduced acute UV effects like erythema, hyperplasia or apoptosis when treated with photoreactivating light
-
?
additional information
?
-
-
CPDs and 6-4PPs play different roles in UV-induced cell death in normal and NER-deficient human cells
-
-
?
additional information
?
-
the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
-
-
?
additional information
?
-
-
the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
-
-
?
additional information
?
-
the first step in the repair mechanism: substrate recognition and binding is s measured by isothermal titration calorimetry
-
-
?
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
predominant role of photolyase is CDP repair of an origin or replication
-
?
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
-
a novel substrate (a modified thymidine 10-mer with a central cyclobutane pyrimidine dimer and all bases, except the one at the 3' end, replaced by 5,6-dihydrothymine) is repaired with an efficiency very similar to that of the conventional substrates (a 10-mer of unmodified thymidines containing a central cyclobutane pyrimidine dimer and an acetone-sensitized thymidine 18-mer containing in average six randomly distributed cyclobutane pyrimidine dimers per strand)
-
-
?
additional information
?
-
-
DNA repair protein
-
-
?
additional information
?
-
-
with photolyase (PL), proteinase K (PK) generates two large daughter proteins (PL-PK1 and PL-PK2), and lower molecular products (PL-PK3 and PL-PK4). PL-PK3 and PL-PK4 may derive from secondary proteolysis of PL-PK1 and PL-PK2, respectively. In photolyase, proteinase K is active at both proteolysis sites. Cleavage to yield PL-chymotrypsin, and PL-PK1 occurs at a common site in photolyase, specifically within the N-terminal, alpha/beta-domain at the W98-N99 and E94-A95 peptide bonds, respectively. PL-PK2 is generated by a cleavage between residues 402 and 404
-
-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
enzyme in complex with CPD moiety, molecular docking study
-
-
?
additional information
?
-
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
CmPHR2 and CmPHR5 specifically repair ssDNA, while the other CRY-DASH (CmPHR6) repairs neither (6-4) photoproduct nor CPD damage in ssDNA or dsDNA. Comparison of the binding constants for ssDNA and dsDNA of Vibrio cholerae CPD photolyase and CRY-DASH by surface plasmon resonance
-
-
?
additional information
?
-
usage of salmon sperm DNA with introduced CPDs (UVC-irradiation) as assay substrate
-
-
?
additional information
?
-
-
usage of salmon sperm DNA with introduced CPDs (UVC-irradiation) as assay substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
cyclobutadipyrimidine in DNA
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
additional information
?
-
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
photolyases utilize near-ultraviolet blue light to specifically repair the major photoproducts of UV-induced damaged DNA. The enzyme specifically repairs CPD lesions
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
the enzyme is involved in biological photoreactivation
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
-
-
-
-
?
cyclobutadipyrimidine (in DNA)
2 pyrimidine residues (in DNA)
Xiphophorus maculatus Jp 163 B
-
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
-
?
cyclobutadipyrimidine in DNA
2 pyrimidine residues in DNA
-
DNA repair activity
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme binds to DNA containing pyrimidine dimers with high affinity and then breaks the cyclobutane ring joining the two pyrimidines of the dimer in a light-dependent reaction, 300-500 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
the enzyme converts the energy of light of near UV to visible wavelengths into chemical energy to break the cyclobutane ring of pyrimidine dimers in DNA and thus prevents the lethal and mutagenic effects of far UV, 200-300 nm
-
-
?
cyclobutadipyrimidine in DNA
?
-
light-dependent(300-600 nm) monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to UV irradiation, 220-320 nm
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
-
DNA repair enzyme can absorb blue/ultraviolet A light as energy and split a pyrimidine dimer induced by ultraviolet radiation. PHR1 gene encodes a functional photolyase. The PHR1 transcripts are specifically enhanced by near-ultraviolet radiation (300-400 nm) and by sunlight
-
-
?
cyclobutadipyrimidine in DNA
pyrimidine residues in DNA
the enzyme is one of the main factors determining UVB sensitivity in Oryza sativa. Cultivar Sasanishiki is resistant to the damaging effects of UVB while cultivar Norin 1 is less resistant. Amino acid position 126 is Arg in cultivar Norin 1 and Gln in cultivar Sasanishiki. The single amino acid alteration from Gln to Arg leads to a deficit of CPD photolyase activity
-
-
?
additional information
?
-
environmental stress enzyme
-
-
?
additional information
?
-
-
environmental stress enzyme
-
-
?
additional information
?
-
light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
-
?
additional information
?
-
-
light-dependent repair of UV-induced damage products in DNA by direct reversal of base damage rather than via excision repair pathways
-
?
additional information
?
-
-
pre-inoculation UV-C (254 nm) treatment of normally susceptible Arabidopsis thaliana accessions induces prolonged, dose-dependent resistance to virulent isolates of the phytopathogenic oomycete Hyaloperonospora parasitica with cyclobutane pyrimidine dimers and (6-4) photoproducts playing a key role in this response
-
-
?
additional information
?
-
-
CryA can repair DNA upon exposure to UVA light similar to other photolyase proteins, CryA represses sexual development under UVA350-370 nm light and exhibits a regulatory function during light-dependent development and DNA repair activity, in the wild type strain mechanisms such as excision repair mask the DNA photolyase activity of CryA
-
-
?
additional information
?
-
the enzyme has blue light photoreceptor activity and CPD photolyase activity. Signaling might be mediated by the PHR besides its effects on the C-terminal extension, conformational changes in cryptochromes upon illumination, overview
-
-
?
additional information
?
-
-
the enzyme has blue light photoreceptor activity and CPD photolyase activity. Signaling might be mediated by the PHR besides its effects on the C-terminal extension, conformational changes in cryptochromes upon illumination, overview
-
-
?
additional information
?
-
-
PHR1 and PHR2 are able to bind the CLOCK protein, a transcription activator controlling the molecular circadian clock. But only for PHR2, the physical interaction with CLOCK represses CLOCK/BMAL1-driven transcription, binding of photolyase per se is not sufficient to inhibit the CLOCK/BMAL1 heterodimer
-
-
?
additional information
?
-
-
CPD photolyase, which rapidly repairs CPDs, is essential for plant survival under sunlight containing UVB
-
-
?
additional information
?
-
-
major pathway to remove UV-induced DNA lesions from the genome
-
?
additional information
?
-
-
photoreduction by intraprotein electron transfer is not part of the photolyase photocycle under physiological conditions
-
-
?
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
?
additional information
?
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
-
enzyme promotes virus survival in the environment
-
?
additional information
?
-
PhrB does not function as a photolyase
-
-
?
additional information
?
-
-
PhrB does not function as a photolyase
-
-
?
additional information
?
-
PhrB does not function as a photolyase
-
-
?
additional information
?
-
the native rice CPD photolyase is phosphorylated, whereas the Escherichia coli-expressed rice CPD photolyase is not
-
-
?
additional information
?
-
-
expression in transgenic mice leads to superior survival, reduced acute UV effects like erythema, hyperplasia or apoptosis when treated with photoreactivating light
-
?
additional information
?
-
-
CPDs and 6-4PPs play different roles in UV-induced cell death in normal and NER-deficient human cells
-
-
?
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
predominant role of photolyase is CDP repair of an origin or replication
-
?
additional information
?
-
-
photolyase repairs nucleosome-free DNA rapidly, while repair of nucleosomes is inhibited severely
-
?
additional information
?
-
-
absolute dependence of catalysis by photolyase on light
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methenyltetrahydrofolate
5,10-methenyltetrahydropterolypolyglutamate
-
-
5,10-methylenetetrahydrofolate
-
antenna pigment in Escherichia coli absorbs blue/near UV light and transfers the excitation energy fast and efficiently to FADH-
7,8-didemethyl-8-hydroxy-5-deazaflavin
7,8-didemethyl-8-hydroxy-5-deazariboflavin
8-hydroxy-5-deazariboflavin
8-hydroxy-7,8-didemethyl-5-deazariboflavin
-
antenna pigment in Anacystis nidulans absorbs blue/near UV light and transfers the excitation energy fast and efficiently to FADH-
8-iodo-8-demethylriboflavin
-
8-iodoflavin
chromophore binding site of Thermus photolyase is reconstited also with a novel synthetic flavin, 8-iodoflavin
ATP
-
stimulates, utilization of ATP for the photorepair process of the pyrimidine dimer containing DNA, not only an allosteric effector
deazaflavin
-
antenna cofactor
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
5,10-methenyltetrahydrofolate
-
-
5,10-methenyltetrahydrofolate
-
5,10-methenyltetrahydrofolate
-
5,10-methenyltetrahydrofolate
-
acts as a light-harvesting pigment
5,10-methenyltetrahydrofolate
-
an electron transfer pathway exists in DASH cryptochrome, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. DASH cryptochrome forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by DASH cryptochrome can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase
5,10-methenyltetrahydrofolate
-
an electron transfer pathway exists in photolyase, where the 5,10-methenyltetrahydrofolate cofactor is photoreduced to 5,10-methylenetetrahydrofolate. Reduction requires the intact tryptophan triad. Photolyase forms 5,10-methylenetetrahydrofolate when treated with UV-A. Light-driven formation of 5,10-methylenetetrahydrofolate by photolyase can be coupled with the formation of NADPH in the presence of 5,10-methylenetetrahydrofolate dehydrogenase
5,10-methenyltetrahydrofolate
-
antenna cofactor
5,10-methenyltetrahydrofolate
-
bound at the interface between N-terminal and C-terminal domain
5,10-methenyltetrahydrofolate
bound at the interface between N-terminal and C-terminal domain
5,10-methenyltetrahydrofolate
-
Cry3
5,10-methenyltetrahydrofolate
FAD and 5,10-methenyltetrahydrofolate act as chromophore and antenna molecules, respectively
5,10-methenyltetrahydrofolate
observed in the cleft between the two domains, where it interacts with two critical amino acid residues, Cys292 and Lys293
5-deazaflavin
-
prosthetic group
7,8-didemethyl-8-hydroxy-5-deazaflavin
-
part of the chromophore
7,8-didemethyl-8-hydroxy-5-deazaflavin
-
essential chromogenic part of the cofactor
7,8-didemethyl-8-hydroxy-5-deazariboflavin
-
-
7,8-didemethyl-8-hydroxy-5-deazariboflavin
chromophore binding site of Thermus photolyase is reconstited also with 7,8-didemethyl-8-hydroxy-5-deazariboflavin (8-HDF). However, in the genome sequence of Thermus thermophilus it is found that the genes essential for the biosynthesis of 8-HDF are missing
8-hydroxy-5-deazaflavin
-
cofactor
8-hydroxy-5-deazaflavin
-
light-harvesting chromophore, not essential for correct folding of the enzyme
8-hydroxy-5-deazaflavin
-
contains the chromophore 8-hydroxy-5-deazaflavin
8-hydroxy-5-deazariboflavin
-
bound at the interface between N-terminal and C-terminal domain
8-hydroxy-5-deazariboflavin
bound at the interface between N-terminal and C-terminal domain
8-hydroxy-5-deazariboflavin
photolyase can bind next to the natural cofactor 8-hydroxy-5-deazariboflavin also FMN
FAD
-
-
FAD
enzyme contains two chromophore cofactors: FAD is a catalytic cofactor which directly contributes to the repair of a pyrimidine-dimer, the other is an unidentified light harvesting cofactor, which absorbs visible light and transfers energy to the catalytic cofactor
FAD
-
only FAD as cofactor, no second cofactor detectable
FAD
-
is indispensable for catalytic activity
FAD
-
the photoexcited FAD cofactor is reduced from the semiquinone or fully oxidized state to the catalytically active FADH- state
FAD
-
the photolyase in its native state contains FAD in the two-electron reduced and deprotonated FADH- form, during purification under aerobic conditions, FADH- is oxidized to the rather stable blue neutral radical
FAD
-
the photolyase in its native state contains FAD in the two-electron reduced and deprotonated FADH- form, during purification under aerobic conditions, FADH- is oxidized to the rather stable blue neutral radical
FAD
-
the purified enzyme binds a FAD, which is in the neutral radical semiquinone form
FAD
the repair reaction involves electron transfer to the cyclobutane pyrimidine dimers from the photoexcited FAD cofactor in its fully reduced form
FAD
-
a second FAD molecule is present in the antenna pigment binding pocket
FAD
-
alpha-helical domain is harboring the FAD cofactor, essential for catalysis
FAD
alpha-helical domain is harboring the FAD cofactor, essential for catalysis
FAD
-
binds the flavin cofactor in a pocket that is conserved in terms of its electronic properties
FAD
-
binds the flavin cofactor in a pocket that is conserved in terms of its electronic properties. W399-W378-W406 may function as potential electron donors to the flavin and are possible candidate tryptophans for light-induced electron transfer
FAD
critical W382 residue relative to the flavin for efficient vectorial electron transfer leading to photoreduction
FAD
-
Cry1, which does not bind to DNA, possesses a strongly reduced surface charge around the FAD binding pocket
FAD
-
large kinetic isotope and pH effects on the rate constants for FAD semiquinone oxidation, which reveal that proton transfer is rate-limiting. Photolyase-specific residues, Trp392 and Gly389, independently ensure a high kinetic barrier to semiquinone reactivity in photolyase, possibly through interactions with the adenine moiety of FAD and/or adjusting the polarity of the binding site. These residues have a much greater impact on semiquinone reactivity than the more FAD proximal Met353 or Ser395
FAD
-
photoreduction of FAD under blue light irradiation is faster in photolyase than in Arabidopsis cry3
FAD
-
photoreduction of FAD under blue light irradiation is faster in photolyase than in Arabidopsis cry3
FAD
-
photolyase's essential cofactor is a non-covalently bound flavin adenine dinucleotide in fully reduced state (FADH-)
FAD
-
photolyase's essential cofactor is a non-covalently bound flavin adenine dinucleotide in fully reduced state (FADH-)
FAD
-
the physiological form of the enzyme contains a fully reduced FAD (FADH-) that is required for its activity both in vivo and in vitro. It binds a cyclobutane pyrimidine dimer (CPD) in DNA independent of light and flips the dimer out of the double helix into the active site cavity to make a stable enzyme-substrate complex. Enzyme usually purified with FAD in the blue neutral radical form. The purified enzyme can hold its radical flavin cofactor unoxidized in aerobic conditions for several days
FAD
-
absorption spectra of FADH+, FADH radical, and FADH- of wild-type and mutant enzymes, overview. All three flavin species and decays to zero upon completion of repair
FAD
FAD and 5,10-methenyltetrahydrofolate act as chromophore and antenna molecules, respectively. The Ver3 chromophore always remains partly (including the semiquinone state) or fully reduced under all experimental conditions tested
FAD
-
light-induced reduction of FAD, and transfer of an electron from the photoexcited reduced FAD to the damaged DNA for cleaving the dimers
FAD
the C-terminal domain frames a concave pocket that holds the FAD cofactor in the U-shaped conformation. The U-shaped FAD is positioned with the isoalloxazine ring buried and the adenine ring solvent-exposed beneath the substrate binding pocket. A salt bridge (Arg396 to Asp427) across the isoalloxazine ring orients the guanidinium to stabilize a semiquinone radical at the C4a position. Cofactor binding and interactions with the enzyme, overview
FAD
the enzyme appears to utilize an unusual, conserved tryptophan dyad as electron transfer pathway to the catalytic FAD cofactor
FAD
the enzyme is capable to photoreduce its catalytic FAD to the active FADH- form. The C-terminal FAD-binding subdomain contains the catalytic cofactor FAD in the U-shaped conformation. FAD-binding site and electron transfer pathway in class II photolyases, overview
FAD
-
the FAD binding region is required for the catalytic activity of DNA photolyase
FAD
bound in a C-terminal alpha-helix cavity, the C-terminal alpha-helical domain consists of 14 alpha-helices. FAD is held in a U-shaped conformation by interaction with 14 conserved amino acid residues
FAD
catalytic cofactor, 4 different redox states of flavin, overview
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state
FAD
dependent on, adopts a uniquely folded configuration at the active site that plays a critical functional role in DNA repair, overview. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. Photolyase utilizes FADH-, not FAD- radical as the active state. Using femtosecond (fs)-resolved spectroscopy and site-directed mutagenesis, the dynamics of class I PL from Escherichia coli (EcPL) in four redox states are investigated
FAD
enzyme SsPL is an unusual photolyase in that it contains two FAD cofactors. One FAD cofactor is part of the active site of the protein and required for both DNA binding and repair. The second cofactor, the putative accessory chromophore, may play a role as a light-harvesting pigment, it is always present in the fully oxidized FAD state. The active site cycles between FADH-, the fully reduced form required for activity, and FADH radical, the one-electron oxidized or semiquinone form, SsPL is isolated with the active site mainly in the FADH· state. The accessory FAD does not appear to readily undergo any reduction-oxidation chemistry, and it is always found in the fully oxidized state
FAD
four redox states of FAD are relevant for the various functions of DNA photolyases: fully reduced FADH- required for DNA photorepair, and the two semireduced radical states FAD- radical and FADH radical formed in electron transfer reactions. Absorption spectra of wild-type EcPL and MTHF antenna-free mutant E109A/N378D EcPL, transient absorption kinetics on nano- and microsecond time scales at six characteristic wavelengths, spectral analysis of transient absorption kinetics, overview
FAD
involved in catalysis, cold-adapted DNA photolyase binds a catalytic flavin adenine dinucleotide (FAD) cofactor noncovalently. UV/Vis and fluorescence spectroscopy reveal that the FAD-binding site in this psychrophilic protein is unique compared to meso/thermophilic PLs. FAD-binding pocket of the CpPL model, overview
FAD
reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA
FAD
steady-state spectra of flavin at various redox states and active-site solvation dynamics in photolyases, overview
FAD
the adenine moiety of FADH- bridges between the electron donating isoalloxazine ring and CPD via two hydrogen bonds, suggesting the presence of electron transfer pathways via adenine
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FAD
the enzyme uses a fully reduced flavin, FADH-, cofactor to repair sunlight-induced DNA lesions
FADH2
-
-
FADH2
-
enzyme contains FADH2 and a second chromophore. Enzyme with a photodecomposed second chromophore retains full activity
FADH2
-
purified enzyme contains a stable neutral radical FAD that is not active in dimer repair. Dimer repair observed with the enzyme containing FAD in the radical form at shorter wavelength is probably photoreduction of the radical FAD followed by dimer repair by enzyme-bound FADH2
FADH2
-
enzyme contains FAD
FADH2
-
enzyme contains FAD
FADH2
-
electron donation by excited states of enzyme-bound FADH2 is the mechanism of flavin photosensitized dimer repair by DNA photolyase
FADH2
-
purified enzyme contains FAD
FADH2
-
catalytic cofactor
FADH2
-
computational calculations demonstrate that the localization of the FADH-donor state on the flavin ring enhances the electronic coupling between the flavin and the dimer by permitting shorter electron-transfer pathways to the dimer that have single through-space jumps. Therefore, in photolyase, the photo-excitation itself enhances the electron transfer rate by moving the electron towards the dimer
FADH2
results indicate that both charge recombination of the primary charge separation state FADH-W382 and electron transfer from W359 to W382 occur with time constants below 4 ps, considerably faster than the initial W382-FADH electron-transfer step.
FADH2
-
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue
FADH2
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R344/D372 and short polypeptide stretches: A377-N378/G381-W382. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N378
FADH2
-
the isoalloxazine ring is sandwiched between a salt bridge comprising an arginine and an aspartate residue: R352/D380 and short polypeptide stretches: A385-N386/G389-W390. Another conserved interaction is a hydrogen bond formed between the N5 nitrogen of the isoalloxazine group and a conserved asparagine: N386. Mutagenesis and ultrafast kinetic spectroscopy revealed a consecutive chain of three conserved tryptophan residues with the order: Y469 -(?)- W314- W367- W390- FAD(H)
FADH2
-
contains the chromophore FADH2
FADH2
-
contains the chromophore FADH2
FADH2
-
the catalytic activity of the enzyme requires fully reduced FAD
FADH2
-
the photoactivation of FADH- immediately preceding the electron transfer is a key step in the repair mechanism
FADH2
-
uses the anionic state of flavin, FADH-,as cofactor
FADH2
-
heterogeneous dynamics continuously tune local configurations to optimize photolyase's function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA
FADH2
-
photoreduction of FADH proceeds along the conserved tryptophan triad W306-W359-W382
flavin
-
prosthetic group
flavin
-
enzyme contains a stable flavin radical, the one-electron reduction potential of the excited quartet state of the flavin radical must be at least 1.23 V more positive than the ground state
flavin
flavin-mononucleotide (FMN), crystal strucutre analysis reveals the binding of flavin mononucleotide as an antenna chromophore
flavin
-
requires fully reduced flavin for photorepair of DNA, full oxidation to FAD is not necessary for biological function, the reaction mechanism involves electron transfer to the substrate from the excited state of the flavin in its fully reduced state FADH- with subsequent electron return within a nanosecond
flavin
-
requires fully reduced flavin for photorepair of DNA, full oxidation to FAD is not necessary for biological function, the reaction mechanism involves electron transfer to the substrate from the excited state of the flavin in its fully reduced state FADH- with subsequent electron return within a nanosecond
FMN
increases the light absorption efficiency of the enzyme, direct electron transfer between FMN and the enzyme is not likely to occur. FMN acts as a highly efficient light harvester that gathers light and transfers the energy to FAD
FMN
photolyase can bind next to the natural cofactor 8-hydroxy-5-deazariboflavin also FMN
folate
-
-
folate
-
enzyme contains folate
methenyltetrahydrofolate
-
-
methenyltetrahydrofolate
-
-
methenyltetrahydrofolate
-
methenyltetrahydrofolate
-
the enzyme utilizes the the antenna cofactor to harvest light energy for the repair of thymine dimers in DNA. For this purpose, the enzyme evolved to bind the cofactor and red-shift its absorption maximum by 25 nm
methenyltetrahydrofolate
-
contains the chromophore methenyltetrahydrofolate
methenyltetrahydrofolate
is the solar panel or photoantenna of the enzyme
methenyltetrahydrofolate
MTHF, the molecule is bound as an antenna molecule and found in substoichiometric amounts
pterin
-
cofactor
pterin
contains not only reduced FAD but also a reduced pterin, or a cofactor with similar properties, as a chromophore
additional information
light-driven blue light flavophotoreceptors all operate from the excited state, whether singlet oxidized (e.g., BLUF and LOV domains) or doublet semiquinone
-
additional information
-
light-driven blue light flavophotoreceptors all operate from the excited state, whether singlet oxidized (e.g., BLUF and LOV domains) or doublet semiquinone
-
additional information
FAD analogues containing either an ethano- or etheno-bridged Ade between the AN1 and AN6 atoms (e-FAD and epsilon-FAD, respectively) are used to reconstitute apo-PL, giving e-PL and epsilon-PL, respectively. The reconstitution yield of e-PL is very poor, suggesting that the hydrophobicity of the ethano group prevents its uptake, while epsilon-PL shows 50% reconstitution yield. The substrate binding constants for epsilon-PL and rPL are identical. epsilon-PL shows a 15% higher steady-state repair yield compared to FAD-reconstituted photolyase (rPL). Evaluation of an epsilon-Ade radical intermediate versus a superexchange mechanism, preparation of apophotolyase (apo-PL) and reconstitution of apo-PL with FAD, e-FAD and epsilon-FAD, overview. Incorporation of the more hydrophobic e-FAD is so inefficient that it can not be made in sufficient quantities to study further. Ligand binding structure analysis
-
additional information
recombinant CpPL (rCpPL) binds two different second cofactor molecules, flavin mononucleotide (FMN) when overexpressed and purified from Escherichia coli BL21(DE3) inclusion bodies, and a folate (possibly MTHF) when overexpressed and purified from Escherichia coli Arctic Express (DE3) cells as a His6-tagged protein or in strain BL21-DE3 cells as a maltose-binding-protein fusion protein. CpPL might be somewhat promiscuous in antenna cofactor binding
-
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evolution
phylogenetic analysis and tree, overview
evolution
phylogenetic analysis, comparison of substrate binding and substrate specificity of class I and class II enzymes, overview. The enzyme shows the overall fold of the photolyase cryptochrome family, surface features of the photolyase-cryptochrome family bound to DNA lesions, overview
evolution
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis strains shows several amino acid differences, strain W1299 has the alterations F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L, and strain W1626 P13S, Q126R and T416P
evolution
-
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1299 strain shows ten amino acid differences, strain W1299 has the alterations: F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L
evolution
-
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1626 strain shows three amino acid differences, strain W1299 has the alterations: P13S, Q126R and T416P
evolution
the PHR/CRY family consists of two major classes, class I and class II, the enzyme from rice belongs to class II
evolution
the PhrB sequence is conserved in both pathogenic and commensal Neisseria species but shares little identity to other bacterial species, phylogenetic analysis, overview. The gonococcal PhrB gene is not a functional orthologue of the Escherichia coli PhrB
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members. The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
evolution
DNA photolyases (PLs) and evolutionarily related cryptochrome (CRY) blue-light receptors form a widespread superfamily of flavoproteins involved in DNA photorepair and signaling functions. They share a flavin adenine dinucleotide (FAD) cofactor and an electron-transfer (ET) chain composed typically of three tryptophan residues that connect the flavin to the protein surface
evolution
the enzyme BcCRY1 belongs to the cryptochrome/photolyase family (CPF), CPD photolyase subfamily
evolution
the enzyme BcCRY2 belongs to the cryptochrome/photolyase family (CPF), cry-DASH subfamily
evolution
the enzyme belongs to the cryptochrome/photolyase family (CPF)
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
evolution
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
evolution
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
evolution
the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. UV is responsible for the formation of two major types of damage-associated photoproducts on DNA: cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone (6-4) photoproducts (Pyr [6-4] Pyr). Two different types of photolyases were eventually discovered: CPD and (6-4) photolyases (EC 4.1.99.13). CPD photolyases repair pyrimidine dimers, while (6-4) photolyases repair Pyr[6-4]Pyr photoproducts
evolution
-
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
-
evolution
-
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1299 strain shows ten amino acid differences, strain W1299 has the alterations: F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L
-
evolution
-
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1626 strain shows three amino acid differences, strain W1299 has the alterations: P13S, Q126R and T416P
-
evolution
-
the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
-
evolution
-
CPD photolyases are highly diversified and can be subdivided into three classes (I to III), as well as single-stranded DNA (ssDNA)-specific PLs. Unrooted phylogenetic tree of the PL-CRY protein family and representative members.The class II PL is distant from the other subfamilies, critical active-site residues that vary between the class I PLs and the other subfamilies, overview
-
evolution
-
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1299 strain shows ten amino acid differences, strain W1299 has the alterations: F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L
-
evolution
-
the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis W1626 strain shows three amino acid differences, strain W1299 has the alterations: P13S, Q126R and T416P
-
evolution
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
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evolution
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phylogenetic analysis, comparison of substrate binding and substrate specificity of class I and class II enzymes, overview. The enzyme shows the overall fold of the photolyase cryptochrome family, surface features of the photolyase-cryptochrome family bound to DNA lesions, overview
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evolution
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the PhrB sequence is conserved in both pathogenic and commensal Neisseria species but shares little identity to other bacterial species, phylogenetic analysis, overview. The gonococcal PhrB gene is not a functional orthologue of the Escherichia coli PhrB
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evolution
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the full-length amino acid sequence of CPD photolyase from Oryza sativa cv. Sasanishiki compared with that of the Oryza meridionalis strains shows several amino acid differences, strain W1299 has the alterations F114L, Q126R, I250M, D258H, F260Y, C305R, V313I, Q367H, Y434F and P495L, and strain W1626 P13S, Q126R and T416P
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evolution
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the enzyme belongs to the photolyase/cryptochrome family of proteins, phylogenetic tree of the cryptochrome/photolyase family (CPF), unrooted phylogenetic tree. The cryptochrome/photolyase family (CPF) includes photoreceptors that perform different functions in different organisms. The class of the CPF known as CRY-DASHs is found in algae, bacteria, plants and animals. CRY-DASH proteins have photolyase activity. Because they specifically repair CPD photoproducts in single-stranded DNA (ssDNA) rather than double-stranded DNA (dsDNA), they are designated as ssDNA photolyases
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evolution
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the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
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evolution
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the enzyme BcCRY1 belongs to the cryptochrome/photolyase family (CPF), CPD photolyase subfamily
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evolution
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the enzyme BcCRY2 belongs to the cryptochrome/photolyase family (CPF), cry-DASH subfamily
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evolution
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the enzyme belongs to the enzyme superfamily of photolyase/cryptochromes. Dynamics of flavin cofactor and its repair photocycles by different classes of photolyases, overview. The unified, bifurcated electron transfer mechanism elucidates the molecular origin of various repair quantum yields of different photolyases from three life kingdoms. Classes of photolyases and structures of CPD and 6-4 photolyases, overview. The diverse subfamily of CPD photolyases consists of classes I, II and III, and ssDNA PLs
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evolution
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phylogenetic analysis and tree, overview
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malfunction
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the CPD photoreactivation rate is undetectable in chloroplasts, mitochondria or nuclei in transgenic rice (AS-D) engineered to express antisense RNA targeting CPD photolyase in wildtype Sasanishiki rice cultivar with low levels of CPD photolyase activity
malfunction
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transient expression in an Escherichia coli strain that lacks its endogenous photolyase, rescues growth of the UV-irradiated bacteria in a light-dependent manner, showing that AMV025 encodes a functional DNA photolyase
malfunction
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using transgenic mice expressing Potorous tridactylus CPD-photolyase, it is shown that Potorous CPD-photolyase affects the clock by shortening the period of behavioral rhythms. Constitutively expressed CPD-photolyase is shown to reduce the amplitude of circadian oscillations in cultured cells and to inhibit CLOCK/BMAL1 driven transcription by interacting with CLOCK. Potorous CPD-photolyase can restore the molecular oscillator in the liver of (clock-deficient) Cry1/Cry2 double knockout mice
malfunction
disruption of Saci 1227 produces an Sulfolobus acidocaldarius strain that exhibits negligible photoreactivation
malfunction
loss of phrB does not result in a mutator phenotype. A Neisseria gonorrhoeae phrB mutant has a reduced colony size that is not a result of a growth defect and the mutant cells exhibit an altered morphology. Although the phrB mutant exhibits increased sensitivity to oxidative killing, it shows increased survival on media containing nalidixic acid or rifampicin, but does not have an increased mutation rate with these antibiotics or spectinomycin and kasugamycin. The phrB mutant shows increased negative DNA supercoiling, but while the protein bound double-stranded DNA, it does not express topoisomerase activity. The Neisseria gonorrhoeae phrB cannot complement an Escherichia coli phrB mutant strain CSR603, and the Neisseria gonorrhoeae phrB mutant is not more sensitive to UV irradiation, independent of visible light exposure, phenotype, overview
malfunction
no changes in UV tolerance and therefore in the effectiveness of photoreactivation are observed for bccry2 deletion or overexpression strains. A retarded lesion spreading, 75% of wild-type, is noted for overexpressing OE::bccry2 strains following inoculation with conidia, overabundance of BcCRY2 causes reduced radial growth rates and delayed initiation of vegetative growth of germinating conidia in axenic culture, and this effect occurs independently of the light conditions
malfunction
the DELTAbccry1 mutant is unable to grow after UV exposure for 6 min, absence of photoreactivation. Overexpression of bccry1 increases UV tolerance, OE::bccry1 conidia show more efficient photoreactivation than the wild-type. Reintroduction of bccry1 into the deficient DELTAbccry1 mutant restores the photorepair activity to wild-type levels. Neither deletion nor overexpression of bccry1 affects differentiation under the conditions tested, the strains show wild-type-like conidiation
malfunction
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disruption of Saci 1227 produces an Sulfolobus acidocaldarius strain that exhibits negligible photoreactivation
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malfunction
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loss of phrB does not result in a mutator phenotype. A Neisseria gonorrhoeae phrB mutant has a reduced colony size that is not a result of a growth defect and the mutant cells exhibit an altered morphology. Although the phrB mutant exhibits increased sensitivity to oxidative killing, it shows increased survival on media containing nalidixic acid or rifampicin, but does not have an increased mutation rate with these antibiotics or spectinomycin and kasugamycin. The phrB mutant shows increased negative DNA supercoiling, but while the protein bound double-stranded DNA, it does not express topoisomerase activity. The Neisseria gonorrhoeae phrB cannot complement an Escherichia coli phrB mutant strain CSR603, and the Neisseria gonorrhoeae phrB mutant is not more sensitive to UV irradiation, independent of visible light exposure, phenotype, overview
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malfunction
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the DELTAbccry1 mutant is unable to grow after UV exposure for 6 min, absence of photoreactivation. Overexpression of bccry1 increases UV tolerance, OE::bccry1 conidia show more efficient photoreactivation than the wild-type. Reintroduction of bccry1 into the deficient DELTAbccry1 mutant restores the photorepair activity to wild-type levels. Neither deletion nor overexpression of bccry1 affects differentiation under the conditions tested, the strains show wild-type-like conidiation
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malfunction
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no changes in UV tolerance and therefore in the effectiveness of photoreactivation are observed for bccry2 deletion or overexpression strains. A retarded lesion spreading, 75% of wild-type, is noted for overexpressing OE::bccry2 strains following inoculation with conidia, overabundance of BcCRY2 causes reduced radial growth rates and delayed initiation of vegetative growth of germinating conidia in axenic culture, and this effect occurs independently of the light conditions
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metabolism
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photoreduction kinetics of class II photolyases are very similar to those of the other classes with even higher photoreduction rates in class II as compared to class I. W399-W378-W406 electron-transfer pathway is conserved among class II CPD photolyase enzymes
metabolism
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photoreduction kinetics of class II photolyases are very similar to those of the other classes with even higher photoreduction rates in class II as compared to class I. W399-W378-W406 electron-transfer pathway is conserved among class II CPD photolyase enzymes
metabolism
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third electron transfer pathway exists in members of the photolyase family that remained undiscovered so far
metabolism
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third electron transfer pathway exists in members of the photolyase family, e.g. DASH cryptochrome, that remained undiscovered so far
physiological function
overexpression of CPD photolyase strongly enhances the repair of cyclobutane pyrimidine dimers and results in a moderate increase of biomass production under elevated UV-B
physiological function
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photolyase can repair UV-damaged DNA in a mechanism requiring light and DNA base flipping, whereas cytochromes cannot repair DNA. Evolution of loop sequence likely plays a key role in functional diversification of cryptochromes and photolyases, through tuning of substrate recognition. Cryptochrome-DASH recognition loop peptide folds 2.5fold faster than its counterpart in photolyase, predominantly due to a lower enthalpy of activation. Binding duplex DNA in the catalytically-active base-flipped conformation imposes significant order on the recognition loop, and a corresponding entropic penalty, which may be surmounted by the more preorganized photolyase recognition loop, but may impose too large a barrier for the more dynamic loop in cryptochrome-DASH
physiological function
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photolyase may function to facilitate DNA repair during UVB exposure. Increased resistance of Photobacterium angustum as compared to Sphingopyxis alaskensis under high UVB doses results from a UVB-induction of CPD photolyase(s) that may directly repair DNA damage and/or act indirectly by enhancing the rate of nucleotide excision repair. Presence of 3 genes coding for DNA photolyase type I enzymes in Photobacterium angustum compared to only 1 for Sphingopyxis alaskensis. Photoresistance strategy may involve a capacity to utilize 3 distinct gene products, including the UVB-induced overexpression of the gene(s). Photolyase activity not only leads to the repair of DNA through a photochemical process, but may also enhance the efficiency of nucleotide excision repair, which is far more efficient in Photobacterium angustum than in Sphingopyxis alaskensis
physiological function
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photolyase may function to facilitate DNA repair during UVB exposure. Increased resistance of Photobacterium angustum as compared to Sphingopyxis alaskensis under high UVB doses results from a UVB-induction of CPD photolyase(s) that may directly repair DNA damage and/or act indirectly by enhancing the rate of nucleotide excision repair. Presence of three genes coding for DNA photolyase type I enzymes in Photobacterium angustum compared to only one for Sphingopyxis alaskensis. Photolyase activity not only leads to the repair of DNA through a photochemical process, but may also enhance the efficiency of nucleotide excision repair, which is far more efficient in Photobacterium angustum than in Sphingopyxis alaskensis
physiological function
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PHR2 protein plays a role in baculovirus DNA repair
physiological function
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PhrB breaks pyrimidine dimers caused by UV exposure, using energy from visible light in the process of photoreactivation. UV-hyper-resistant strain contains a single mutation: a 1 bp deletion in the intergenic region directly upstream of the mutT-phrB operon, encoding nudix hydrolase and photolyase
physiological function
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structural similarity between the larger N-terminal domain of primase (PriL) with the active site region of DNA photolyase
physiological function
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very similar to plant cryptochromes
physiological function
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the Cc-phr2 gene product can complement an Escherichia coli photolyase deficiency and can repair T-T dimers in vitro, showing that the Cc-PHR2 protein has photolyase activity
physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
physiological function
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photolyases use visible light to repair ultraviolet-induced DNA damage. PHR2 binds the CLOCK protein and represses CLOCK/BMAL1-driven transcription, it also affects the oscillation of immortalized mouse embryonic fibroblasts, suggesting that PHR2 can regulate the molecular circadian clock
physiological function
the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
physiological function
the enzyme PhrB has a role in maintaining DNA supercoiling that is important for normal cell physiology
physiological function
ambient ultraviolet B (UVB) radiation induces lethal effects in the two-spotted spider mite Tetranychus urticae, whereas photoreactivation by irradiation with ultraviolet A and visible light (VIS) plays an important role to increase survival of mites irradiated by UVB. DNA lesions, cyclobutane pyrimidine dimers (CPDs), photoproducts linearly increase with the UVB dose. The CPDs are repaired after exposure to visible light. DNA damage and CPD photo enzymatic repair (PER) is significant for survival in this mite under ambient UVB radiation, but gene expression of CPD photolyase is unaffected by irradiation with UVB and VIS, while UVB-irradiated larvae survival rate decreases as the UVB cumulative dose increases, CPD frequency increased with the UVB cumulative dose
physiological function
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. BcCRY2 belongs to the cry-DASH proteins and is dispensable for photorepair but performs regulatory functions by repressing conidiation in white and especially black/NUV light. Neither light nor the White Collar complex (WCC) is essential for the repression of conidiation through BcCRY2 when bccry2 is constitutively expressed. BcCRY2 affects the transcript levels of both WCC-induced and WCC-repressed genes, suggesting a signaling function downstream of the WCC. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY2 acts as a cryptochrome with a signaling function in regulating photomorphogenesis (repression of conidiation). BcCRY2 functions in the regulation of vegetative growth, overview. BcCRY2 has a negative impact on conidiation, the R/G-rich region of BcCRY2 is not essential for the regulation of conidiation. No impact of BcCRY2 on sclerotial development
physiological function
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. CRY1 (BcCRY1), a cyclobutane pyrimidine dimer (CPD) photolyase, acts as the major enzyme of light-driven DNA repair (photoreactivation) and has no obvious role in signaling. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY1 acts as the major photolyase in photoprotection, BcCRY1 is crucial for photorepair, overview. No impact of BcCRY1 on sclerotial development
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Class I photolyase shows electron tunneling and high repair efficiency
physiological function
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Class I photolyase shows electron tunneling and high repair efficiency
physiological function
CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum
physiological function
CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum. Consistent with their role in global gene regulation, cryptochrome genes (CmPHR2, CmPHR3 and CmPHR7) are differentially regulated, suggesting that they have a potential role in light-dependent transcriptional regulation in Cyanidioschyzon merolae
physiological function
DNA photolyase is a structure-specific DNA repair enzyme that reverses one of the most common types of UV damage in DNA molecules, the cis-syn cyclobutylpyrimidine dimer (CPD)
physiological function
photolyase, a class of flavoproteins, restores damaged DNA through absorption of blue light, CPD photolyase uses blue light to repair ultraviolet-induced DNA damage, cyclobutane pyrimidine dimers (CPDs), repair dynamics and mechanisms, cyclic electron-transfer reaction photocycle, overview
physiological function
photolyases are structure-specific DNA-repair enzymes that repair DNA lesions that have been induced by ultraviolet (UV) light. Escherichia coli DNA photolyase is a DNA-repair enzyme that repairs cyclobutane pyrimidine dimers (CPDs) which are formed on DNA upon exposure of cells to ultraviolet light. The photolyase catalyzes the CPD monomerization by a light-driven electron-transfer mechanism after the enzyme-substrate complex has formed. The enzyme requires flipping of the CPD site into an extrahelical position. The photolyase is unique in that it requires the two dimerized pyrimidine bases to flip rather than just a single damaged base
physiological function
residue Gln336 is important for the repair activity of CPD photolyase in Dunaliella salina and may represent key amino acid residues under salt stress
physiological function
the photoinduced electron transfer (ET) reaction of cyclobutane pyrimidine dimer (CPD) photolyase plays an essential role in its DNA repair reaction
physiological function
UV irradiation converts two adjacent pyrimidines, including thymines, to a cyclobutane pyrimidine dimer (CPD), and the enzyme photolyase uses blue light energy to break the two abnormal bonds joining the thymines and thus converts the thymine dimer to two normal thymines. Photolyase therefore repairs DNA and eliminates the harmful effects of UV light. The blue light-absorbing component of photolyase are chromophores. Photolyase from Escherichia coli contains two chromophores, which are two-electron reduced flavin adenine dinucleotide (FADH-) and methenyltetrahydrofolate (folate). The folate acts like a solar panel, absorbing light and transferring the excitation energy to FADH-. The flavin is the actual catalyst, and upon excitation by energy transfer from folate (and less efficiently by direct absorption of a photon) it carries out the repair reaction on the CPD by a radical mechanism through a cyclic redox reaction
physiological function
UV is responsible for the formation of damage-associated photoproducts on DNA: cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone (6-4) photoproducts (Pyr [6-4] Pyr). CPD photolyases repair pyrimidine dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum
physiological function
UV-induced lesions can be repaired by enzymes called photolyases. DNA photolyases use blue/near-UV light to remove these lesions using a process referred to as photoreactivation. CPD photolyases specifically repair CPD lesions in DNA
physiological function
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UVB-induced DNA lesions in Xiphophorus fishes are thought to primarily be repaired via light dependent CPD and 6-4PP specific photolyases, cf. EC 4.1.99.13
physiological function
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UVB-induced DNA lesions in Xiphophorus fishes are thought to primarily be repaired via light dependent CPD and 6-4PP specific photolyases, cf. EC 4.1.99.13
physiological function
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CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
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physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
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physiological function
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CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair. Class I photolyase shows electron tunneling and high repair efficiency
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physiological function
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the photoinduced electron transfer (ET) reaction of cyclobutane pyrimidine dimer (CPD) photolyase plays an essential role in its DNA repair reaction
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physiological function
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CPD photolyase is a blue-light-activated enzyme that repairs ultraviolet-induced DNA damage which occurs in the form of cyclobutane pyrimidine dimers (CPDs). The enzyme uses a fully reduced flavin (FADH-) cofactor to repair sunlight-induced DNA lesions
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physiological function
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PhrB breaks pyrimidine dimers caused by UV exposure, using energy from visible light in the process of photoreactivation. UV-hyper-resistant strain contains a single mutation: a 1 bp deletion in the intergenic region directly upstream of the mutT-phrB operon, encoding nudix hydrolase and photolyase
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physiological function
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the enzyme catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA
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physiological function
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in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
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physiological function
Xiphophorus maculatus Jp 163 B
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UVB-induced DNA lesions in Xiphophorus fishes are thought to primarily be repaired via light dependent CPD and 6-4PP specific photolyases, cf. EC 4.1.99.13
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physiological function
Vibrio cholerae serotype O1 ATCC 39315 / El Tor Inaba N16961
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CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum
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physiological function
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the enzyme PhrB has a role in maintaining DNA supercoiling that is important for normal cell physiology
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physiological function
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DNA photolyase is a structure-specific DNA repair enzyme that reverses one of the most common types of UV damage in DNA molecules, the cis-syn cyclobutylpyrimidine dimer (CPD)
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physiological function
-
in plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity
-
physiological function
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CRY-DASH proteins have photolyase activity, photolyases repair Pyr<>Pyr dimers. Photolyases repair ultraviolet-induced DNA damage by a process known as photoreactivation using photons absorbed from the blue end of the light spectrum. Consistent with their role in global gene regulation, cryptochrome genes (CmPHR2, CmPHR3 and CmPHR7) are differentially regulated, suggesting that they have a potential role in light-dependent transcriptional regulation in Cyanidioschyzon merolae
-
physiological function
-
CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
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physiological function
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conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. CRY1 (BcCRY1), a cyclobutane pyrimidine dimer (CPD) photolyase, acts as the major enzyme of light-driven DNA repair (photoreactivation) and has no obvious role in signaling. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY1 acts as the major photolyase in photoprotection, BcCRY1 is crucial for photorepair, overview. No impact of BcCRY1 on sclerotial development
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physiological function
-
conidiation in plant-pathogenic leotiomycete Bortrytis cinerea is induced by black/near-UV light, whose sensing is attributed to the action of cryptochrome/photolyase family (CPF) proteins. BcCRY2 belongs to the cry-DASH proteins and is dispensable for photorepair but performs regulatory functions by repressing conidiation in white and especially black/NUV light. Neither light nor the White Collar complex (WCC) is essential for the repression of conidiation through BcCRY2 when bccry2 is constitutively expressed. BcCRY2 affects the transcript levels of both WCC-induced and WCC-repressed genes, suggesting a signaling function downstream of the WCC. The enzyme is dispensable for photoinduction by black/NUV light. BcCRY2 acts as a cryptochrome with a signaling function in regulating photomorphogenesis (repression of conidiation). BcCRY2 functions in the regulation of vegetative growth, overview. BcCRY2 has a negative impact on conidiation, the R/G-rich region of BcCRY2 is not essential for the regulation of conidiation. No impact of BcCRY2 on sclerotial development
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physiological function
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CPD photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer (CPD) photoproduct using blue light. The FAD cofactor, conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a unique folded configuration at the active site that plays a critical functional role in DNA repair
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additional information
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electron-tunneling pathways and functional role of adenine moiety of wild-type and mutant enzymes, overview
additional information
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illumination leads to the neutral semiquinoid state of the photolyase with maxima at 590 nm and 632 nm, respectively. Stabilizing role of asparagine N403 in class II photolyases. The innermost tryptophan W381 is crucial for catalytic activity, electron transfer pathway along the tryptophan catalytic triad W388-W360-W381 to FAD
additional information
illumination leads to the neutral semiquinoid state of the photolyase with maxima at 590 nm and 632 nm, respectively. Stabilizing role of asparagine N403 in class II photolyases. The innermost tryptophan W381 is crucial for catalytic activity, electron transfer pathway along the tryptophan catalytic triad W388-W360-W381 to FAD
additional information
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repair mechanism and the substrate specificity that distinguish enzyme CPD-PHR from enzyme (6-4) PHR, EC 4.1.99.13, which uniquely repairs (6-4) photoproducts, using Fourier transform infrared spectroscopy, overview
additional information
structure-activity relationships in class II PHRs, overview. Structural comparisons with prokaryotic class I CPD PHRs identify differences in the binding site for UV-damaged DNA substrate
additional information
analysis of flavin in various redox states and the active-site solvation dynamics in photolyases, and dynamics of a similar CPD biomimetic system but with low repair efficiency, overview. High repair quantum yield by CPD photolyases. Ultrafast active-site solvation dynamics in photolyases. Dynamic solvation in binding and active sites plays a critical role in protein recognition and enzyme reaction and such local motions optimize spatial configurations and minimize energetic pathways. X-ray structures and molecular dynamics (MD) simulations show certain water molecules trapped at the active sites besides charged and polar amino acids surrounding the functional chromophore of FADH-. Thus, upon excitation the local polar environments at the active sites proceed to a series of relaxations
additional information
comparison of the photoactive center of wild-type Escherichia coli enzyme with the one from Arabidopsis thaliana CRY1 enzyme
additional information
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comparison of the photoactive center of wild-type Escherichia coli enzyme with the one from Arabidopsis thaliana CRY1 enzyme
additional information
during purification, the flavin undergoes changes in oxidation state and as a consequence the enzyme may exhibit colors ranging from purple to orange. Three-dimensional structure and structural basis for the proposed reaction mechanism, overview
additional information
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during purification, the flavin undergoes changes in oxidation state and as a consequence the enzyme may exhibit colors ranging from purple to orange. Three-dimensional structure and structural basis for the proposed reaction mechanism, overview
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme AnPL from Anacystis nidulans is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme EcPL from Escherichia coli is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme from Sulfolobus tokodaii is hyperthermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
enzyme structure comparisons and molecular modeling, overview. The enzyme from Thermus thermophilus is thermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
additional information
homology analysis of PL protein structures spanning 70°C in growth temperature supports the data that the structure of cold-adapted DNA photolyase CpPL is quite different from warm-adapted DNA photolyases. Homology modeling of CpPL using CPD-PL from Sulfolobus tokodaii (StPL, 2E0I. PDB, chain A) as a template
additional information
in class I EcPL, the initial electron injection adopts dominant tunneling pathways directly from LfH- to CPD. Reaction free energy profile along the reaction coordinate for EcPL CPD repair, overview
additional information
light-induced conformational changes in the plant cryptochrome photolyase homology region resolved by selective isotope labeling and infrared spectroscopy
additional information
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light-induced conformational changes in the plant cryptochrome photolyase homology region resolved by selective isotope labeling and infrared spectroscopy
additional information
reduced anionic flavin adenine dinucleotide (FADH-) is the critical cofactor in DNA photolyase (PL) for the repair of cyclobutane pyrimidine dimers (CPD) in UV-damaged DNA. The initial step involves photoinduced electron transfer from FADH- radical to the CPD. The adenine (Ade) moiety is nearly stacked with the flavin ring, an unusual conformation compared to other FAD-dependent proteins
additional information
the crystal structure of Anacystis nidulans photolyase with CPD complex shows that the Ade moiety of FADH- is at van der Waals distances with both base moieties of CPD, 3.1 A to the 5' side and 3.2 A to 3'. The first carbon atom is linked to the isoalloxazine ring at 3.6 A
additional information
the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview
additional information
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the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview
additional information
to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated
additional information
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to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated
additional information
-
homology analysis of PL protein structures spanning 70°C in growth temperature supports the data that the structure of cold-adapted DNA photolyase CpPL is quite different from warm-adapted DNA photolyases. Homology modeling of CpPL using CPD-PL from Sulfolobus tokodaii (StPL, 2E0I. PDB, chain A) as a template
-
additional information
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the crystal structure of Anacystis nidulans photolyase with CPD complex shows that the Ade moiety of FADH- is at van der Waals distances with both base moieties of CPD, 3.1 A to the 5' side and 3.2 A to 3'. The first carbon atom is linked to the isoalloxazine ring at 3.6 A
-
additional information
-
enzyme structure comparisons and molecular modeling, overview. The enzyme AnPL from Anacystis nidulans is mesophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Sulfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
-
additional information
-
to analyze the UV-induced DNA lesion repair mechanism, the excited states of the active site (including the electron donor and acceptor) is calculated
-
additional information
-
illumination leads to the neutral semiquinoid state of the photolyase with maxima at 590 nm and 632 nm, respectively. Stabilizing role of asparagine N403 in class II photolyases. The innermost tryptophan W381 is crucial for catalytic activity, electron transfer pathway along the tryptophan catalytic triad W388-W360-W381 to FAD
-
additional information
-
the enzymatic activity and thermodynamics of substrate binding for the enzyme from Sulfolobus solfataricus are directly compared to the enzyme from Escherichia coli, overview. Turnover numbers and catalytic activity are virtually identical, but organic co-solvents may be necessary to maintain activity of the thermophilic protein at higher temperatures. UV-damaged DNA binding to the thermophilic protein is less favorable by about 2 kJ/mol. The enthalpy of binding is about 10 kJ/mol less exothermic for the thermophile, but the amount and type of surface area buried upon DNA binding appears to be somewhat similar. The most important finding is observed when ionic strength studies are used to separate binding interactions into electrostatic and nonelectrostatic contributions, DNA binding to the thermophilic protein appears to lack the electrostatic contributions observed with the mesophilic protein. Reported differences between mesophilic and thermophilic enzymes include an increase in the number of ion pairs/salt bridges, better packing of hydrophobic amino acids, and increased hydrogen bonding for the thermophilic proteins. Comparison of the enthalpy of binding. Analysis of enzyme-substrate interactions, overview
-
additional information
-
enzyme structure comparisons and molecular modeling, overview. The enzyme from Thermus thermophilus is thermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
-
additional information
-
enzyme structure comparisons and molecular modeling, overview. The enzyme from Sulfolobus tokodaii is hyperthermophile. There is a significant adenine-mediated superexchange contribution to the electron transfer repair reaction when CPD is complexed with the photolyases in Anacystis nidulans (mesophile) and in the two extremophiles (Thermus thermophilus and Solfolobus tokodaii) at their physiological temperatures. In contrast, the predominant electron transfer mechanism in the Escherichia coli photolyase at its physiological temperature (37°C) is direct electron transfer, with only about 3% of the strongest electron transfer pathways mediated by adenine. Role of adenine in the CPD repair, adenine flipping
-
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W356F
-
photobleaching of 5,10-methenyltetrahydrofolate under UV-A irradiation is strongly reduced in the mutant compared with wild-type. The amount of 5,10-methenyltetrahydrofolate after UV-A irradiation is reduced by 64% for wild-type and by 20% for the mutant. Increase in the amount of oxidized FAD under UV-A irradiation due to electron donation to 5,10-methenyltetrahydrofolate by residual FADH- but a lack of photoreduction of the flavin caused by the interrupted tryptophan triad
W432F
-
photobleaching of 5,10-methenyltetrahydrofolate under UV-A irradiation is strongly reduced in the mutant compared with wild-type
R350A
-
conserved arginine forms a salt bridge with phosphate+1. Among several active-site mutants this R/A mutant is found to exhibit the greatest effect by lowering the selectivity toward cyclobutane-pyrimidine dimer-containing DNA 32-fold and the quantum yield of CPD cleavage from 98% to about 60%
deltaphrA
-
Rhodobacter sphaeroides mutant cells lacking the PhrA gene show a significant reduced survival rate after UV-illumination
Q336H
site-directed mutagenesis of the alpha13 conserved amino acid residue
E109D
-
mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined
E109Q
-
mutant enzyme is unable to bind the methenyltetrahydrofolate cofactor under any conditions examined
L375H
-
binds methenyltetrahydrofolate more weakly than wild-type enzyme
N341A
-
life-time of 2.9 ns compared to 1.3 ns for the wild-type enzyme
N378D
site-directed mutagenesis, the asparagine facing the N5 of the FAD isoalloxazine is replaced by aspartic acid, known to protonate FAD- radical (formed by electron transfer from the tryptophan chain) in plant cryptochromes (CRYs). But the mutant protein does not show this protonation. EcPL mutant protein approaches the flavin with similar kinetics to that of the aspartic acid at the corresponding position in plant CRY, but is unable to fully transfer the proton to N5 of the flavin, resulting in a FAD radical with unusual spectral properties. Possibly, the pKa values of FADH radical and/or this aspartic acid in the EcPL N378D mutant protein differ from those in native plant CRY, such that proton transfer is energetically disfavored. Absorption kinetics compared to wild-type
W277E
-
the binding affinity for CPD substrate is lower for 1000fold, although the photochemical properties and the quantum yields for catalyses (under the irradiation wavelengths at 366nm and 384 nm) of the mutant is indistinguishable from the wild-type enzyme
W277R
-
the binding affinity for CPD substrate is lower for 300fold, although the photochemical properties and the quantum yields for catalyses (under the irradiation wavelengths at 366nm and 384 nm) of the mutant is indistinguishable from the wild-type enzyme
N403A
replacement of asparagine N403 for either a non-polar alanine or a hydrophobic leucine causes complete loss of the catalytic FAD during purification by size exclusion chromatography
N403L
replacement of asparagine N403 for either a non-polar alanine or a hydrophobic leucine causes complete loss of the catalytic FAD during purification by size exclusion chromatography
W360F
mutation of the medial tryptophan, W360, gives a 22fold decrease of photoreduction activity relative to the wild type enzyme, no major build-up of the semiquinoid FADH radical species can be observed for W360F
W381F
the mutation causes complete loss of photoreduction activity and a loss of 70% of incorporation of the catalytic FAD compared to the wild-type enzyme
N403A
-
replacement of asparagine N403 for either a non-polar alanine or a hydrophobic leucine causes complete loss of the catalytic FAD during purification by size exclusion chromatography
-
N403L
-
replacement of asparagine N403 for either a non-polar alanine or a hydrophobic leucine causes complete loss of the catalytic FAD during purification by size exclusion chromatography
-
W360F
-
mutation of the medial tryptophan, W360, gives a 22fold decrease of photoreduction activity relative to the wild type enzyme, no major build-up of the semiquinoid FADH radical species can be observed for W360F
-
W381F
-
the mutation causes complete loss of photoreduction activity and a loss of 70% of incorporation of the catalytic FAD compared to the wild-type enzyme
-
Q126R
the mutation leads to a reduction of enzymatic activity
Q296H
the mutation leads to a reduction of enzymatic activity
S267A
site-directed mutagenesis, the mutant enzyme is phosphorylated
S494A
site-directed mutagenesis, the mutant enzyme is phosphorylated
S504A
site-directed mutagenesis, the mutant enzyme is phosphorylated
S5A
site-directed mutagenesis, the mutant enzyme is phosphorylated
S7A
site-directed mutagenesis, the mutant enzyme is not phosphorylated
S84A
site-directed mutagenesis, the mutant enzyme is phosphorylated
T115A
site-directed mutagenesis, the mutant enzyme is phosphorylated
S267A
-
site-directed mutagenesis, the mutant enzyme is phosphorylated
-
S504A
-
site-directed mutagenesis, the mutant enzyme is phosphorylated
-
S5A
-
site-directed mutagenesis, the mutant enzyme is phosphorylated
-
S84A
-
site-directed mutagenesis, the mutant enzyme is phosphorylated
-
T115A
-
site-directed mutagenesis, the mutant enzyme is phosphorylated
-
A385S
-
is blue after purification as the wild-type. Partial formation of oxidized FAD is evident after 2 days as with the wild-type. Shows enhanced semiquinone stability
E283A
-
the mutation impairs enzyme activity by diminishing the quantum yield for the repair reaction by 60%
G389N
-
is yellow-green after purification, significantly less semiquinone present. Reaction time of ca. 3 days is required for complete conversion of semiquinone to oxidized FAD. Kinetic stability of the semiquinone is significantly reduced, semiquinone oxidation rates more closely resemble that in cryptochrome-DASH
M353Q
-
is blue after purification as the wild-type. Partial formation of oxidized FAD is evident after 2 days as with the wild-type. Has little impact on semiquinone stability
R350A
-
the mutation demonstrates a 60% decrease in quantum yield, which indicates that Arg350 plays a key role in stabilizing the dimer
W392Y
-
is yellow-green after purification, significantly less semiquinone present. Reaction time of ca. 2 days is required for complete conversion of semiquinone to oxidized FAD. Kinetic stability of the semiquinone is significantly reduced, semiquinone oxidation rates more closely resemble that in cryptochrome-DASH
R46E
R46E mutant which lacks a conserved arginine in the binding site for the antenna chromophore shows no flavin-mononucleotide and discloses an eightfold lower activity at 450 nm (blue light) wheras at 370 nm (UV-A light) its activity is only three times lower than wildtype enzyme
H354A
-
affinity to substrate is comparable to wild-type enzyme, no activity
H358A
-
affinity to substrate is comparable to wild-type enzyme, no activity
L355A
-
low affinity to the substrate
Q288A
-
affinity to substrate is comparable to wild-type enzyme
W291A
-
affinity to substrate is comparable to wild-type enzyme, mutant retains some activity
W398A
-
affinity to substrate is comparable to wild-type enzyme, mutant retains some activity
W395R
-
the mutation compromises FAD binding of wild type enzyme without significantly affecting the overall conformation of photolyase, the mutant has essentially lost its DNA binding activity, and the residual activity that remains cannot discriminate between damaged and undamaged DNA
W395R
-
fully binds methenyltetrahydrofolate but not fully reduced FADH-, life-time of 2.9 ns
W395R
-
the mutation compromises FAD binding of wild type enzyme without significantly affecting the overall conformation of photolyase, the mutant has essentially lost its DNA binding activity, and the residual activity that remains cannot discriminate between damaged and undamaged DNA
-
E109A
-
site-directed mutagenesis, inactive mutant
E109A
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non-5,10-methenyltetrahydrofolate-binding mutant
E109A
-
is catalytically active but unable to bind the second cofactor methenyltetrahydrofolate
E109A
-
lacks the antenna cofactor
E274A
-
site-directed mutagenesis of a residue near the substrate side
E274A
-
site-directed mutagenesis of an active site residue
E274A
site-directed mutagenesis of an active site residue near the substrate side, has critical effect on repair efficiency
H44F
-
binds and retains methenyltetrahydrofolate under normal reconstitution conditions
H44F
-
mutant enzyme retains no methenyltetrahydrofolate upon purification
M345A
-
site-directed mutagenesis of an active site residue
M345A
site-directed mutagenesis of an active site residue, has a poor effect on repair efficiency
N108L
-
binds and retains methenyltetrahydrofolate under normal reconstitution conditions
N108L
-
mutant enzyme retains no methenyltetrahydrofolate upon purification
N378C
-
site-directed mutagenesis of a residue near the flavin cofactor side
N378C
-
site-directed mutagenesis of an active site residue
N378C
site-directed mutagenesis of an active site residue near the cofactor side, has critical effect on repair efficiency
N378S
-
the mutation stabilizes the oxidized state of the flavin
N378S
-
the recombinant mutant photolyase contains oxidized FAD (FADox) but not FADH after routine purification procedures, the mutant protein contains FADH in vivo as the wild type enzyme, the mutant photolyase is photoreducible and capable of binding cyclobutadipyrimidine dimers in DNA, but catalytically inert
N378S
-
mutant shows no stable radical state of the cofactor FADH. Furthermore, catalytic activity is lost
R226A
-
site-directed mutagenesis of an active site residue
R226A
site-directed mutagenesis of an active site residue, has a poor effect on repair efficiency
R342A
conserved arginine forms a salt bridge with phosphate+1. Among several active-site mutants this R/A mutant is found to exhibit the greatest effect by lowering the selectivity toward cyclobutane-pyrimidine dimer-containing DNA 32-fold and the quantum yield of CPD cleavage from 98% to about 60%
R342A
-
site-directed mutagenesis of an active site residue
R342A
site-directed mutagenesis of an active site residue, has a poor effect on repair efficiency
W306F
-
non-photoreducible mutant, like the wild-type enzyme the mutant enzyme carries out at least 25 rounds of photorepair at the same rate
W306F
in the W306F mutant, the terminal tryptophan W306 is replaced by an isosteric phenylalanine that is much harder to oxidize, thus leaving the electron-transfer chain cut off after the second tryptophan W359, the W359 radical formed in the W306F mutant photolyase is in its neutral form already at 10 ns after excitation
W306F
naturally occuring mutant
W306F
-
lacks the ultimate intrinsic electron donor (terminal tryptophan replaced by redox inert phenylalanine), shows an important deprotonation/recombination process with a time constant of 0.85 ns
additional information
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mutation of Q411 and K414 affect the affinity toward cyclobutane-pyrimidine dimer-containing DNA
additional information
generation of deletion mutant DELTAbccry1 and overexpression strain OE::bccry1, phenotype, overview
additional information
generation of deletion mutant DELTAbccry1 and overexpression strain OE::bccry1, phenotype, overview
additional information
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generation of deletion mutant DELTAbccry1 and overexpression strain OE::bccry1, phenotype, overview
additional information
generation of deletion mutant DELTAbccry2 and overexpression strain OE::bccry2, phenotype, overview
additional information
generation of deletion mutant DELTAbccry2 and overexpression strain OE::bccry2, phenotype, overview
additional information
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generation of deletion mutant DELTAbccry2 and overexpression strain OE::bccry2, phenotype, overview
additional information
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generation of deletion mutant DELTAbccry1 and overexpression strain OE::bccry1, phenotype, overview
-
additional information
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generation of deletion mutant DELTAbccry2 and overexpression strain OE::bccry2, phenotype, overview
-
additional information
comparison of repair activity of the photolyase in the wild-type strain PGEX-4T-1-DsPHR2 and the mutant strain PGEX-4T-1-DsPHR2-Q336H in vitro and in vitro and under different salt concentrations, overview. The mutant shows reduced repair activity compared to wild-type, and the survival rate declines rapidly as salinity increased in the mutant Q336H, while in the wild-type strain, there is no change in the survival rate
additional information
mutation of Q403 and K406 affect the affinity toward cyclobutane-pyrimidine dimer-containing DNA
additional information
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transgenic mice are generated with a transgene for a marsupial CPD photolyase. These mice exhibit a 40% increase of repair for CPD lesions in intact skin and cultured fibroblasts that is accompanied by an improved resistance against acute UV-induced effects like erythema (sunburn), epidermal hyperplasia or apoptosis. Expression of the CPD photolyase in mice efficiently suppresses the formation of skin carcinomas
additional information
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by evolutionary sequence analysis it is shown that Met353 of the CPD photolyase derived from Anacystis nidulans is perfectly conserved throughout the putative class I CPD photolyase
additional information
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Met-353 of the CPD photolyase has been perfectly conserved throughout the putative class I CPD photolyases and plays a pivotal role in the biological function of DNA photolyase
additional information
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deletion of phr1 gene abolishes photoreactivation of UVC (200 to 280 nm)-inhibited spores
additional information
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to assess phr1 photosensory function, fluence response curves of the light-regulated promoter are tested in null mutant (deltaphr1) strains. Photoinduction of the phr1 promoter in deltaphr1 strains are more than 5fold more sensitive to light than that in the wild type, whereas in PHR1-overexpressing lines the sensitivity to light increases about 2fold
additional information
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immobilization of recombinant purified DNA photolyase using avidin-biotin-based immobilization method with neutravidin-modified BioCap chip as a sensor surface
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