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ATP + H2O
ADP + phosphate
ATP + H2O
AMP + diphosphate
GTP + H2O
GDP + phosphate
additional information
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
at optimal assay conditions, the RadADa presynaptic complex is able to hydrolyze ATP efficiently with ssDNA cofactors of 940 nt and greater. Circular and linearized M13 ssDNA demonstrate the same ability to stimulate ATP hydrolysis as a linearized dsDNA of this phage, whereas the supercoiled dsDNA (replicative form I) is a weak cofactor due to the only partial denaturation at 90°C
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ATP + H2O
ADP + phosphate
the highly purified enzyme exusively catalyzes single-stranded DNA-dependent ATP hydrolysis, which monitors presynaptic recombinational complex formation, at temperatures above 65°C. The RadA protein alone efficiently promotes the strand exchange reaction at the range of temperatures from 80 to 90°C, i.e., at temperatures approaching the melting point of DNA
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
ssDNA-dependent ATPase activity
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
both ATP hydrolysis and DNA strand exchange requires accessibility to an active conformation similar to the crystallized ATPase-active form in the presence of ATP, Mg2+ and K+
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ATP + H2O
ADP + phosphate
single-stranded DNA-dependent ATPase
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ATP + H2O
ADP + phosphate
the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature
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ATP + H2O
ADP + phosphate
the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
DNA-dependent ATPase, D-loop formation, and strand exchange activities. The enzyme is involved in homologous recombination
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ATP + H2O
ADP + phosphate
DNA-dependent ATPase, D-loop formation, and strand exchange activities
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ATP + H2O
ADP + phosphate
the central core domain of RadA is essential for the strand exchange activity and that the N-terminal domain contributes to the enhancement of the reaction efficiency
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the RadA protein is a DNA-dependent ATPase, forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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ATP + H2O
ADP + phosphate
ssDNA-dependent ATPase activity
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ATP + H2O
ADP + phosphate
the ATPase activity of SsoRadA is ssDNA-dependent. It is suggested that the recombinase first binds ATP, then binds DNA. ATP hydrolysis has no effect on ssDNA binding. After the protein is bound to ssDNA, it hydrolyzes ATP
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ATP + H2O
ADP + phosphate
the DNA exchange protein RadA displays preference for binding to DNA sequences that are rich in G residues, and under-represented in A and C residues
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ATP + H2O
ADP + phosphate
the RadA protein is a ssDNA-dependent ATPase. ATP hydrolysis is less efficient in the presence of double-stranded DNA, and almost no hydrolysis occurs in the absence of DNA. It forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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ATP + H2O
ADP + phosphate
SsoRadA ssDNA-dependent ATPase activity
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the ATPase activity of SsoRadA is ssDNA-dependent. It is suggested that the recombinase first binds ATP, then binds DNA. ATP hydrolysis has no effect on ssDNA binding. After the protein is bound to ssDNA, it hydrolyzes ATP
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ATP + H2O
ADP + phosphate
the RadA protein is a DNA-dependent ATPase, forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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ATP + H2O
ADP + phosphate
the RadA protein is a ssDNA-dependent ATPase. ATP hydrolysis is less efficient in the presence of double-stranded DNA, and almost no hydrolysis occurs in the absence of DNA. It forms a nucleoprotein filament on DNA, and catalyzes DNA pairing and strand exchange
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ATP + H2O
ADP + phosphate
the DNA exchange protein RadA displays preference for binding to DNA sequences that are rich in G residues, and under-represented in A and C residues
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
SsoRadA ssDNA-dependent ATPase activity
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
AMP + diphosphate
the enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA
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ATP + H2O
AMP + diphosphate
ATPase activity is most efficient in presence of ssDNA, it is considerably reduced in presence of dsDNA and virtually no ATP is hydrolysed in absence of DNA. The enzyme catalyses efficient D-loop formation and strand exchange at temperatures of 60-70°C, capable of promoting strand transfer through at least 1200 bp of duplex DNA
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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GTP + H2O
GDP + phosphate
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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performance of transformation and survival assays, DNA helicase assays, ATP hydrolysis assays, and protein-DNA or protein-protein interactions analysis
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additional information
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performance of transformation and survival assays, DNA helicase assays, ATP hydrolysis assays, and protein-DNA or protein-protein interactions analysis
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additional information
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performance of transformation and survival assays, DNA helicase assays, ATP hydrolysis assays, and protein-DNA or protein-protein interactions analysis
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additional information
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an NADH-coupled assay is used to measure the ATPase activity of RadA, in the presence or absence of various DNA cofactors, circular ssDNA (jX174 virion) and dsDNA (jX174 RF DNA). DNA substrate specificity of RadA binding, overview. The wild-type RadA protein preferentially binds single-strand DNA in the presence of ADP. Binding preference for by poly(dT) by RadA and also by RecA. RadA is observed to bind poly(dT)30 when flanked on both 5' and 3' ends by 30 nucleotides of natural DNA sequence. Catalysis of RecA-mediated strand-exchange reactions between 5386 nucleotide circular jX174 ssDNA and linear duplex DNA in the presence of ATP and an ATP-regeneration system, ATP hydrolysis in reactions including RecA, SSB and RadA
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additional information
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an NADH-coupled assay is used to measure the ATPase activity of RadA, in the presence or absence of various DNA cofactors, circular ssDNA (jX174 virion) and dsDNA (jX174 RF DNA). DNA substrate specificity of RadA binding, overview. The wild-type RadA protein preferentially binds single-strand DNA in the presence of ADP. Binding preference for by poly(dT) by RadA and also by RecA. RadA is observed to bind poly(dT)30 when flanked on both 5' and 3' ends by 30 nucleotides of natural DNA sequence. Catalysis of RecA-mediated strand-exchange reactions between 5386 nucleotide circular jX174 ssDNA and linear duplex DNA in the presence of ATP and an ATP-regeneration system, ATP hydrolysis in reactions including RecA, SSB and RadA
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additional information
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monomeric RAD51 is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. AMPPNP binds to RAD51, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
?
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
?
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
?
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to generate C-terminal hydrazides in proteins, an efficient intein-based preparation method is developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method is expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. The versatile preparation method can expand the utilization of protein C-terminal hydrazides in protein preparation and modification. Method evaluation, overview. RadA, which had appreciable splicing efficiency with non-native extein residues. RadA intein is more tolerant to the nature of the residue at the -1 position, its rate of cleavage is slower than that of the VMA and GyrA inteins. Hence, its splicing typically requires conditions such as high temperature or partial denaturation. Generalizability of the method
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additional information
?
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monomeric RadA-ct is able to bind ATP, ADP, AMPPNP, GTP and GDP in an Mg2+-dependent manner. AMP is not able to bind to the protein indicating that both the beta- and gamma-phosphates are essential for this interaction. ADP and GDP bind to RadA with approximately twice the affinity of their triphosphate equivalents, possibly due to the different conformation of the side chain of Phe140 between the di- and triphosphorylated nucleotide complexes, with the additional negative charge of the gamma-phosphate repelling the aromatic ring. AMPPNP binds to mutant RadA-ct, but with reduced affinity in comparison with ATP. This is likely to be caused by the inability of the nitrogen between the band gamma-phosphates to form a hydrogen bond with the backbone amide of Gly141 as observed in the complex with ATP. Comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. The guanine-containing nucleotides bind to the monomeric form of RadA and RAD51 with a somewhat higher affinity than the adenine-containing equivalents. Selectivity for ATP over GTP appears to be mediated by the binding of the second protomer, which forms specific interactions with ATP but not with GTP
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additional information
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enzyme RadA binds both to ssDNA and dsDNA. The highly thermostable RadA protein from the archaeon Pyrococcus woesei enhances the specificity of simplex and multiplex PCR assays
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additional information
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enzyme RadA binds both to ssDNA and dsDNA. The highly thermostable RadA protein from the archaeon Pyrococcus woesei enhances the specificity of simplex and multiplex PCR assays
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additional information
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formation of SsoRadA-ssDNA complexes resulting in SsoRadA nucleoprotein filaments
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additional information
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formation of SsoRadA-ssDNA complexes resulting in SsoRadA nucleoprotein filaments
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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formation of SsoRadA-ssDNA complexes
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additional information
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formation of SsoRadA-ssDNA complexes
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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formation of SsoRadA-ssDNA complexes resulting in SsoRadA nucleoprotein filaments
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additional information
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formation of SsoRadA-ssDNA complexes
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additional information
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methods for DNA and ATP binding assays, strand invasion and exchange, and ATPase assays, detailed overview
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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additional information
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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?
additional information
?
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The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview
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evolution
cis-splicing of the engineered RadAmin intein is very efficient and indistinguishable from that of PhoRadA intein, suggesting that the removed disordered loop is a mere remnant from the endonuclease domain that was lost during evolution
evolution
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the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
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the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
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the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
the enzyme belongs to the RecA/RadA family of recombinase proteins, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
the enzyme belongs to the RecA/RadA family of recombinase proteins, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
evolution
Bacillus subtilis encodes three branch migration translocases: RuvAB, RecG, and RadA, i.e. Sms
evolution
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the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
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evolution
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Bacillus subtilis encodes three branch migration translocases: RuvAB, RecG, and RadA, i.e. Sms
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evolution
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cis-splicing of the engineered RadAmin intein is very efficient and indistinguishable from that of PhoRadA intein, suggesting that the removed disordered loop is a mere remnant from the endonuclease domain that was lost during evolution
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evolution
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the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea
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malfunction
a null radA mutation impairs chromosomal transformation, in the absence of RadA competent cells require the RecG translocase for natural chromosomal transformation. A RadA/SmsC4 mutation impairs chromosomal and plasmid transformation. Enzyme mutants RadA C13A or C13R fail to interact with RecA and do not promote unwinding of a non-cognate 3'-tailed or 5'-fork DNA substrate. Enzyme mutants RadA C13A and C13R hydrolyse ATP in a ssDNA-dependent manner. Mutant RadA C13A interacts with itself but does not interact with RecA. RadA C13A and C13R variants preferentially bind ssDNA, albeit with lower efficiency than the wild-type enzyme. RadA C13A and C13R mutants bind natural ssDNA and partially displace SsbA
malfunction
loss of radA, by itself, reduces recovery of genetic rearrangements at tandem-repeated sequences, which are promoted by defects in the replication fork helicase, DnaB. In addition, loss of RadA reduces homologous recombination when in combination with loss of RuvAB or RecG as measured by conjugation with Hfr donors (RuvAB and RecG are DNA motor proteins that branch-migrate recombination intermediates such as Holliday junctions during the late stages of homologous recombination). Mutations in the Walker A, KNRFG and zinc finger motifs abolish RadA's branch migration activity in RecA-coupled reactions and lead to the accumulation of strand exchange intermediate species
malfunction
translocase depletion in tumor cell lines leads to the accumulation of RAD51 on chromosomes, forming complexes that are not associated with markers of DNA damage. Combined depletion of RAD54L and RAD54B and/or artificial induction of RAD51 overexpression blocks replication and promotes chromosome segregation defects. Induction of nondamage-associated RAD51 foci is associated with reduced cell growth. Replication defects and mitotic defects associated with accumulation of nondamage-associated RAD51 complexes, overview
malfunction
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a null radA mutation impairs chromosomal transformation, in the absence of RadA competent cells require the RecG translocase for natural chromosomal transformation. A RadA/SmsC4 mutation impairs chromosomal and plasmid transformation. Enzyme mutants RadA C13A or C13R fail to interact with RecA and do not promote unwinding of a non-cognate 3'-tailed or 5'-fork DNA substrate. Enzyme mutants RadA C13A and C13R hydrolyse ATP in a ssDNA-dependent manner. Mutant RadA C13A interacts with itself but does not interact with RecA. RadA C13A and C13R variants preferentially bind ssDNA, albeit with lower efficiency than the wild-type enzyme. RadA C13A and C13R mutants bind natural ssDNA and partially displace SsbA
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metabolism
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nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
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nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
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nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
metabolism
RAD54 family translocases prevent accumulation of nondamage-associated RAD51 complexes in MCF-7 cells
metabolism
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nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
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metabolism
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nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion
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physiological function
archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. This DNA-repair function also plays a key role in the resistance of cancer cells to chemotherapy and radiotherapy and in the resistance of bacterial cells to antibiotics
physiological function
homologous recombinational repair is an essential mechanism for repair of double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial role in this process, forming filaments that utilize ATP to mediate their interactions with singleand double-stranded DNA
physiological function
play a key role in DNA repair by forming helical nucleoprotein filaments which promote a hallmark strand exchange reaction between homologous DNA substrates
physiological function
RecA family protein filaments may function as rotary motors
physiological function
recombinases of the RecA family play vital roles in homologous recombination, a high-fidelity mechanism to repair DNA double-stranded breaks. These proteins catalyze strand invasion and exchange after forming dynamic nucleoprotein filaments on ssDNA
physiological function
the enzyme is involved in homologous recombination
physiological function
the enzyme promotes recombination at temperatures approaching the DNA melting point
physiological function
homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor
physiological function
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homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
physiological function
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homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
physiological function
homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
physiological function
homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
physiological function
homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
physiological function
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homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essentialmediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
physiological function
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the archaeon may not encode a eukarya-type of NER (nucleotide excision repair) pathway because depleting each of the eukaryal NER homologues XPD, XPB and XPF does not impair the DNA repair capacity in their mutants. But among seven homologous recombination proteins, including RadA, Hel308/Hjm, Rad50, Mre11, HerA, NurA and Hjc, only the Hjc nuclease is dispensable for cell viability. Analysis of genetic mechanisms of DNA repair in this model organism, overview
physiological function
RadA can bind to single-stranded DNA and stimulate branch migration to increase the rate of homologous recombination. RadA allows branch migration to occur even when RecA is missing, but RadA is unable to begin strand exchange if RecA is not present. The process of branch migration stabilizes the DNA molecules during homologous recombination and may also allow the repaired DNA strand to engage the machinery that copies DNA. In vitro RecA mediates strand exchange, a key step of recombination. RadA has an effect on the structure of RecA. The wild-type RadA protein preferentially binds single-strand DNA in the presence of ADP, exhibits ATPase activity stimulated by DNA, and increases the rate of RecA-mediated recombination in vitro by stimulation of branch migration. Branch migration can be mediated by RadA even in the absence of RecA and is highly directional in nature, with preferential extension of the heteroduplex in the 5' to 3' direction, relative to the initiating single-strand, this is codirectional with that of RecA-mediated strand exchange. DNA branch migration and exchange mechanism, overview
physiological function
the strand exchange protein RAD51 functions to promote genome stability by repairing DNA double strand breaks (DSB) and damaged replication forks. RAD51 repairs damage by forming helical nucleoprotein filaments on tracts of ssDNA. Such tracts form by 5'-3' processing of DNA ends formed by DSBs, and also as a consequence of replication fork collapse or blockage. The ssDNA-specific binding protein RPA binds rapidly and with high specificity to ssDNA tracts and, with the help of mediator proteins, promotes the recruitment of RAD51. Following nucleoprotein filament formation, RAD51 carries out a search for homologous dsDNA sequences and then promotes invasion of target duplex leading to the exchange of DNA strands that forms heteroduplex DNA within an intermediate called the displacement loop (D-loop). The ssDNA strand displaced from the target duplex during heteroduplex DNA formation also binds RPA. Subsequent stages of the recombination process result in repair of damage without loss or rearrangement of DNA sequences. RAD54L and RAD54B counteract genome-destabilizing effects of direct binding of RAD51 to dsDNA in human tumor cells. Thus, in addition to having genome-stabilizing DNA repair activity, human RAD51 has genome-destabilizing activity when expressed at high levels, as is the case in many human tumors. Within the RPA-positive subpopulation, induction of RAD51 overexpression was associated with redistribution of RPA from the diffuse staining pattern to punctate foci, suggesting that they form on undamage dsDNA, with subsequent local accumulation of RPA foci as a consequence of replisome collisions with preformed RAD51 fibers
physiological function
wild-type RadA interacts with and inhibits the ATPase activity of RecA (BG214). RadA and its mutant variants, C13A and C13R, bound to the 5'-tail of a DNA substrate, unwind DNA in the 5'->3' direction. RecA interacts with and loads wild-type RadA to promote unwinding of a non-cognate 3'-tailed or 5'-fork DNA substrate. Wild-type RadA interaction with RecA is crucial to recruit the former onto D-loop DNA, and both proteins in concert catalyse D-loop extension to favour integration of ssDNA during chromosomal transformation. But RadA inhibits the ATPase activity of RecA. Proposed model for the action of the 5'->3' RadA helicase in coordination with RecA during natural transformation and in double strand break repair, overview. RadA is crucial for chromosomal transformation, but is essential in the DELTArecG background. Functional analysis, detailed overview
physiological function
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recombinases of the RecA family play vital roles in homologous recombination, a high-fidelity mechanism to repair DNA double-stranded breaks. These proteins catalyze strand invasion and exchange after forming dynamic nucleoprotein filaments on ssDNA
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physiological function
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homologous recombinational repair is an essential mechanism for repair of double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial role in this process, forming filaments that utilize ATP to mediate their interactions with singleand double-stranded DNA
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physiological function
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RecA family protein filaments may function as rotary motors
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physiological function
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homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase
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physiological function
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wild-type RadA interacts with and inhibits the ATPase activity of RecA (BG214). RadA and its mutant variants, C13A and C13R, bound to the 5'-tail of a DNA substrate, unwind DNA in the 5'->3' direction. RecA interacts with and loads wild-type RadA to promote unwinding of a non-cognate 3'-tailed or 5'-fork DNA substrate. Wild-type RadA interaction with RecA is crucial to recruit the former onto D-loop DNA, and both proteins in concert catalyse D-loop extension to favour integration of ssDNA during chromosomal transformation. But RadA inhibits the ATPase activity of RecA. Proposed model for the action of the 5'->3' RadA helicase in coordination with RecA during natural transformation and in double strand break repair, overview. RadA is crucial for chromosomal transformation, but is essential in the DELTArecG background. Functional analysis, detailed overview
-
physiological function
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homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor
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additional information
catalytic site structure analysis, the scissile peptide bond between Met-1 and Ala1 of minimized RadA intein is in the usual transconformation
additional information
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catalytic site structure analysis, the scissile peptide bond between Met-1 and Ala1 of minimized RadA intein is in the usual transconformation
additional information
determination of structures of one of inteins with high splicing efficiency, the RadA intein from Pyrococcus horikoshii (PhoRadA). The solution NMR structure and the crystal structures elucidate the structural basis for its high efficiency, precise interactions between N-extein and the intein, NMR structure determination and structure-function analysis, overview. Comparison between the NMR and crystal structures of PhoRadA intein
additional information
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determination of structures of one of inteins with high splicing efficiency, the RadA intein from Pyrococcus horikoshii (PhoRadA). The solution NMR structure and the crystal structures elucidate the structural basis for its high efficiency, precise interactions between N-extein and the intein, NMR structure determination and structure-function analysis, overview. Comparison between the NMR and crystal structures of PhoRadA intein
additional information
Sulfolobus tokodaii encodes four putative RadA paralogues, RadA paralogue stRadC2 is involved in DNA recombination via interaction with recombinase RadA and the Holliday junction Hjc. stRadC2 inhibits the strand exchange activity of RadA and facilitates Hjc-mediated Holliday junction DNA cleavage in vitro. stRadC2 may act as an anti-recombination factor in DNA recombinational repair in Sulfolobus tokodaii
additional information
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Sulfolobus tokodaii encodes four putative RadA paralogues, RadA paralogue stRadC2 is involved in DNA recombination via interaction with recombinase RadA and the Holliday junction Hjc. stRadC2 inhibits the strand exchange activity of RadA and facilitates Hjc-mediated Holliday junction DNA cleavage in vitro. stRadC2 may act as an anti-recombination factor in DNA recombinational repair in Sulfolobus tokodaii
additional information
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the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
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the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
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the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
additional information
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comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
additional information
comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
additional information
homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
additional information
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homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
additional information
RAD51 fibers may be helical nucleoprotein filaments
additional information
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RAD51 fibers may be helical nucleoprotein filaments
additional information
RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC
additional information
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RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC
additional information
splicing of RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. This splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies coevolution of the parasitic intein and its host protein may provide another means of post-translational control. Homology models for the RadA extein and intein are generated separately based on the closest templates for the extein: PDB ID 2ZUB, and for the intein: PDB ID 4E2T, molecular dynamics simulations, overview. The catalytic residues of the intein are located on the extein-intein interface, revealing the possibility for 3D extein-intein interactions affecting intein catalysis. Conserved residues of the intein C153, H245, H312, H323 and N324 are oriented toward the RadA exteins
additional information
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splicing of RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. This splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies coevolution of the parasitic intein and its host protein may provide another means of post-translational control. Homology models for the RadA extein and intein are generated separately based on the closest templates for the extein: PDB ID 2ZUB, and for the intein: PDB ID 4E2T, molecular dynamics simulations, overview. The catalytic residues of the intein are located on the extein-intein interface, revealing the possibility for 3D extein-intein interactions affecting intein catalysis. Conserved residues of the intein C153, H245, H312, H323 and N324 are oriented toward the RadA exteins
additional information
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homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
-
additional information
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the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
-
additional information
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comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
-
additional information
-
homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
-
additional information
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comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
-
additional information
-
comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
-
additional information
-
homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
-
additional information
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comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
-
additional information
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catalytic site structure analysis, the scissile peptide bond between Met-1 and Ala1 of minimized RadA intein is in the usual transconformation
-
additional information
-
determination of structures of one of inteins with high splicing efficiency, the RadA intein from Pyrococcus horikoshii (PhoRadA). The solution NMR structure and the crystal structures elucidate the structural basis for its high efficiency, precise interactions between N-extein and the intein, NMR structure determination and structure-function analysis, overview. Comparison between the NMR and crystal structures of PhoRadA intein
-
additional information
-
the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain
-
additional information
-
homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
-
additional information
-
comparisons of nucleotide-bound enzyme and enzyme mutant structure, overview. Nucleotide binding might have an allosteric and/or co-operative effect on the binding to FxxA sequences and plays an additional role in regulating the oligomeric structures of the recombinase
-
additional information
-
splicing of RadA intein located in the ATPase domain of the hyperthermophilic archaeon Pyrococcus horikoshii is strongly regulated by the native exteins, which lock the intein in an inactive state. This splicing trap occurs through interactions between distant residues in the native exteins and the intein, in three-dimensional space. The exteins might thereby serve as an environmental sensor, releasing the intein for full activity only at optimal growth conditions for the native organism, while sparing ATP consumption under conditions of cold-shock. This partnership between the intein and its exteins, which implies coevolution of the parasitic intein and its host protein may provide another means of post-translational control. Homology models for the RadA extein and intein are generated separately based on the closest templates for the extein: PDB ID 2ZUB, and for the intein: PDB ID 4E2T, molecular dynamics simulations, overview. The catalytic residues of the intein are located on the extein-intein interface, revealing the possibility for 3D extein-intein interactions affecting intein catalysis. Conserved residues of the intein C153, H245, H312, H323 and N324 are oriented toward the RadA exteins
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additional information
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homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
-
additional information
-
homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
-
additional information
-
homology modeling of the Hvo RadA primary sequence using the Pfu RadA structure (PDB ID 1PZN) chain A as the highest scoring template. Consistent with its function as a recombinase, ATP and DNA binding motifs are apparent which have a well-conserved sequence composition despite the common skews in overall amino acid usage typically observed in halophilic proteins
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x * 49400, recombinant enzyme, SDS-PAGE
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x * 49400, recombinant enzyme, SDS-PAGE
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?
x * 38400, SDS-PAGE, calculated from sequence
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x * 35867, calculated from sequence
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x * 35900, about, sequence calculation
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x * 35900, about, sequence calculation
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?
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x * 35900, about, sequence calculation
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?
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x * 35900, about, sequence calculation
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?
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x * 35867, calculated from sequence
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?
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x * 35900, about, sequence calculation
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oligomer
the enzyme forms rings and nucleoprotein filaments. In the presence of ssDNA and ATP-gamma-S helical nucleoprotein filament structures are observed. RadA forms filaments on ssDNA. No protein-DNA complexes are formed on dsDNA. Such preference for binding ssDNA may allow targeting of RadA protein to the ssDNA. In absence of DNA, RadA shows a tendency to form ring-like structures in vivo. Ring structures may be the inactive storage form of the recombinase that are transported to the sites of DNA repair and then converted into functional helical nucleoprotein filaments when loaded onto ssDNA
oligomer
stable selfassociation of the RadA proteins
oligomer
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Sso RadA proteins are capable of self-assembling into long and fine helical filaments up to 1 lm in length. This unusual protein filament exists not only in solution but also in RadA protein crystals without addition of any nucleotide cofactor. Sso RadA protein filament will dissemble upon incubation with ssDNA substrate and AMP-PNP, and then form only nucleoprotein filaments
polymer
the enzyme can selfpolymerize into left-handed helical filaments
polymer
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the enzyme can selfpolymerize into left-handed helical filaments
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undecamer
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additional information
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enzyme domain organization, overview
additional information
RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain
additional information
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RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain
additional information
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RadA has four well-conserved motifs: a potential C4-type zinc-binding motif at the N-terminal domain, a central canonical RecA-like ATPase domain (H1-H4 motifs) and KNRFG motif, and the P/LonC domain at the C-terminus domain
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additional information
RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC
additional information
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RadA is a 460 amino acid protein that has three well-conserved domains also found in other proteins, as well as a 5-amino acid motif highly conserved among radA orthologs. The N-terminal 30 amino acids form a putative zinc-finger domain with a C4 motif, CXXC-Xn-CXXC
additional information
RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
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RadA multimerizes into a ring-like structure in the absence of DNA and nucleoside cofactor
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additional information
enzyme domain organization, structure comparisons, overview
additional information
enzyme domain organization, structure comparisons, overview
additional information
primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein
additional information
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primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein
additional information
highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529)
additional information
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highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529)
additional information
the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
additional information
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the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
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additional information
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primary structures of PhoRadA intein, secondary structure based on the determined NMR model. Comparison between the NMR and crystal structures of PhoRadA intein
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additional information
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the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
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additional information
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the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
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additional information
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the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
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additional information
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the C-terminal ATPase domain RadA is monomeric, analysis of binding of ATP and other nucleotides to nonoligomeric RadA
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additional information
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highly electrostatic secondary structure elements of the ATPase domain of RadA: helix 1 (D352-K367), loop 1 (R496-R503) and loop 2 (E524-D529)
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additional information
enzyme domain organization, structure comparisons, overview
additional information
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enzyme domain organization, structure comparisons, overview
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additional information
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enzyme domain organization, overview
additional information
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enzyme domain organization, overview
additional information
enzyme domain organization, overview
additional information
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enzyme domain organization, overview
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C13A
site-directed mutagenesis of the tetracysteine motif, the mutant variant binds ssDNA, and this interaction stimulates its ATPase activity. Wild-type RadA interacts with and inhibits the ATPase activity of RecA, but mutant RadA C13A fails to do so
C13R
site-directed mutagenesis of the tetracysteine motif, the mutant variant binds ssDNA, and this interaction stimulates its ATPase activity
K104R
site-directed mutagenesis, the mutant variant in the Walker A (radA1041 [K104R]) motif forms a complex with RecA
C13A
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site-directed mutagenesis of the tetracysteine motif, the mutant variant binds ssDNA, and this interaction stimulates its ATPase activity. Wild-type RadA interacts with and inhibits the ATPase activity of RecA, but mutant RadA C13A fails to do so
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C13R
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site-directed mutagenesis of the tetracysteine motif, the mutant variant binds ssDNA, and this interaction stimulates its ATPase activity
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K104R
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site-directed mutagenesis, the mutant variant in the Walker A (radA1041 [K104R]) motif forms a complex with RecA
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C28Y
RadA mutant C28Y retains the ATPase activity but is defective in DNA binding
K108R
the mutation at the Walker A sequence results in a dominant-negative RadA allele in Escherichia coli, it shows highly reduced DNA binding compared to wild-type
K258A
the mutation in the KNRFG motif negates RadA function and is partially dominant in vivo, it shows highly reduced DNA binding compared to wild-type
S372A
the RadA mutant retains ATPase and DNA-binding activities similar to wild-type
D246A
loss of binding a second Mg2+. Initial ATP turnover rate is reduced by about 20-fold
D246N
initial ATP turnover rate is reduced by about 20-fold
D302K
mutant protein shows comparable strand exchange efficiencies in the presence of either potassium or sodium
E151D
mutant protein retains potassium preference in promoting strand exchange. Reduced ATPase activity and normal strand exchange activity
E151K
mutant protein retains potassium preference in promoting strand exchange. Reduced ATPase activity and normal strand exchange activity
E354A
site-directed mutagenesis, mutant M9, matuation of a residue involved in ATPase function, and coordination of the nucleophilic water molecule
E360A
site-directed mutagenesis, mutant M5, mutation of residues involved in exstein-intein interaction
E360A/R363A/E364A
site-directed mutagenesis, mutant M3, mutation of residues involved in exstein-intein interaction
E364A
site-directed mutagenesis, mutant M7, mutation of residues involved in exstein-intein interaction
E57A/K58A/R60A/E61A
site-directed mutagenesis, mutant M12, mutation of a residue that aisnot expected to be in proximity to intein catalytic residues
E77A/K79A/E80A
site-directed mutagenesis, mutant M11, mutation of a residue that aisnot expected to be in proximity to intein catalytic residues
I169M/Y201A/V202Y/E219S/D220A/K221M
site-directed mutagenesis, construction of mutant, termed HumRadA2, that resembles human RAD51. The mutant shows reduced thermal stability compared to wild-type, while the crystal structure of this mutant shows no structural changes in the ATP-binding site with respect to the wild-type. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant monomeric HumRadA2, overview
Q465A
site-directed mutagenesis, mutant M10, matuation of a residue involved in ATPase function, and coordination of the nucleophilic water molecule
R358A
site-directed mutagenesis, mutant M4, mutation of residues involved in exstein-intein interaction
R358A/E360A/R363A/E364A
site-directed mutagenesis, mutant M1, mutation of residues involved in exstein-intein interaction
R358A/R361A
site-directed mutagenesis, mutant M2, mutation of residues involved in exstein-intein interaction
R361A
site-directed mutagenesis, mutant M6, mutation of residues involved in exstein-intein interaction
R503A
site-directed mutagenesis, mutant M8, mutation of residues involved in exstein-intein interaction
I169M/Y201A/V202Y/E219S/D220A/K221M
E354A
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site-directed mutagenesis, mutant M9, matuation of a residue involved in ATPase function, and coordination of the nucleophilic water molecule
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E360A
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site-directed mutagenesis, mutant M5, mutation of residues involved in exstein-intein interaction
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I169M/Y201A/V202Y/E219S/D220A/K221M
-
site-directed mutagenesis, construction of mutant, termed HumRadA2, that resembles human RAD51. The mutant shows reduced thermal stability compared to wild-type, while the crystal structure of this mutant shows no structural changes in the ATP-binding site with respect to the wild-type. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant monomeric HumRadA2, overview
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R358A
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site-directed mutagenesis, mutant M4, mutation of residues involved in exstein-intein interaction
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R361A
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site-directed mutagenesis, mutant M6, mutation of residues involved in exstein-intein interaction
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R503A
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site-directed mutagenesis, mutant M8, mutation of residues involved in exstein-intein interaction
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K120A
reduced ATPase activity, mutant K120A is able to bind ssDNA with ATP, ADP, or ATPgammaS under saturating protein conditions, but failed to bind well at subsaturating concentrations with ATP or ATPgammaS
K120R
reduced ATPase activity, mutant only binds ATP in the presence of ssDNA
K27R
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, exhibits weaker affinity to dsDNA as compared to wild-type protein
K60R
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, binds dsDNA as well as wild-type protein
R217A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, association and dissociation kinetics largely identical or similar to that of the wild-type protein, exhibits weaker affinity to dsDNA as compared to wild-type protein
R217K
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, mutant exhibits slower ssDNA association rate, surface plasmon resonance binding signals is similar to that of wild-type protein, exhibits weaker affinity to dsDNA as compared to wild-type protein
R223A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, association and dissociation kinetics largely identical or similar to that of the wild-type protein, 90100% reduction of the surface plasmon resonance binding signal, mutants is defective in dsDNA binding
R223K
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, surface plasmon resonance binding signals is similar to that of wild-type protein, mutants is defective in dsDNA binding
R229A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, association and dissociation kinetics largely identical or similar to that of the wild-type protein, 90100% reduction of the surface plasmon resonance binding signal, mutants is defective in dsDNA binding
R229K
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, surface plasmon resonance binding signals is similar to that of wild-type protein, mutants is defective in dsDNA binding
K120A
-
reduced ATPase activity, mutant K120A is able to bind ssDNA with ATP, ADP, or ATPgammaS under saturating protein conditions, but failed to bind well at subsaturating concentrations with ATP or ATPgammaS
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K120R
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reduced ATPase activity, mutant only binds ATP in the presence of ssDNA
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I169M/Y201A/V202Y/E219S/D220A/K221M
-
site-directed mutagenesis, construction of mutant, termed HumRadA2, that resembles human RAD51. The mutant shows reduced thermal stability compared to wild-type, while the crystal structure of this mutant shows no structural changes in the ATP-binding site with respect to the wild-type. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant monomeric HumRadA2, overview
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I169M/Y201A/V202Y/E219S/D220A/K221M
-
site-directed mutagenesis, construction of mutant, termed HumRadA2, that resembles human RAD51. The mutant shows reduced thermal stability compared to wild-type, while the crystal structure of this mutant shows no structural changes in the ATP-binding site with respect to the wild-type. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant monomeric HumRadA2, overview
-
I169M/Y201A/V202Y/E219S/D220A/K221M
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site-directed mutagenesis, construction of mutant, termed HumRadA2, that resembles human RAD51. The mutant shows reduced thermal stability compared to wild-type, while the crystal structure of this mutant shows no structural changes in the ATP-binding site with respect to the wild-type. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant monomeric HumRadA2, overview
-
I169M/Y201A/V202Y/E219S/D220A/K221M
-
site-directed mutagenesis, construction of mutant, termed HumRadA2, that resembles human RAD51. The mutant shows reduced thermal stability compared to wild-type, while the crystal structure of this mutant shows no structural changes in the ATP-binding site with respect to the wild-type. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant monomeric HumRadA2, overview
-
K27A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, 90100% reduction of the surface plasmon resonance binding signal, exhibits weaker affinity to dsDNA as compared to wild-type protein
K27A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, mutant exhibits slower ssDNA association rate
K60A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein
K60A
mutant does not produced a D-loop product as compared to that of the wild type SsoRadA protein, mutants is defective in dsDNA binding
additional information
mutation of serine 372 of RadA, comparable in alignments to the active site serine of Lon, does not affect RadA genetic function and this serine is not conserved among RadAs
additional information
-
mutation of serine 372 of RadA, comparable in alignments to the active site serine of Lon, does not affect RadA genetic function and this serine is not conserved among RadAs
additional information
-
construction of monomeric form of RAD51 in which BRC repeat 4 from BRCA2 is covalently linked to the N-terminus of the ATPase domain of human RAD51. Fluorescence-based thermal shift and isothermal titration calorimetric analyses of nucleotide binding to recombinant mutant RAD51-BRC4, overview
additional information
structure-based rational design of a functional minimized RadA intein with mutation C1A/T1A (intein/extein) and residues 121-130 removed, the structure of the minimized RadA intein reveals the precise interactions between N-extein and the intein, overview. Effects at the -1 position of N-extein and significant improvement of the splicing efficiency of a less robust splicing variant by eliminating the unfavorable extein-intein interactions observed in the structure. Construction of mutant PhoRad Intein harboring the C1A mutation in the intein and a two-residue C-extein with a mutation of Thr to Ala (T+1A), aimed at prevention of splicing and cleavage
additional information
-
structure-based rational design of a functional minimized RadA intein with mutation C1A/T1A (intein/extein) and residues 121-130 removed, the structure of the minimized RadA intein reveals the precise interactions between N-extein and the intein, overview. Effects at the -1 position of N-extein and significant improvement of the splicing efficiency of a less robust splicing variant by eliminating the unfavorable extein-intein interactions observed in the structure. Construction of mutant PhoRad Intein harboring the C1A mutation in the intein and a two-residue C-extein with a mutation of Thr to Ala (T+1A), aimed at prevention of splicing and cleavage
additional information
construction of enzyme mutants MBP-RadAC46, MBP-Arg-RadA, MBP-Glu-RadA, MBP-Asn-RadA, MBP-Pro-RadA, MBP-Asp-RadA, MBP-Ser-RadA, MBP-Cys-RadA, MBP-Gly-RadA, MBP-Arg-RadADELTAC46, MBP-Glu-RadADELTAC46, MBP-Asn-RadADELTAC46, MBP-Pro-RadADELTAC46, MBP-Asp-RadADELTAC46, MBP-Ser-RadADELTAC46, MBP-Cys-RadADELTAC46, and MBP-Gly-RadADELTAC46
additional information
isolation of the C-terminal ATPase domain by removing the N-terminal domain and the linker that contains the FxxA oligomerisation sequence. To facilitate crystallisation, the unstructured L2 DNA-binding loop is also removed, creating a construct denoted as RadA-ct, analysis of structures of RadA-ct bound to ATP, ADP, AMPPNP and GTP, cyrstal structure of phosphate-bound RadA-ct, overview
additional information
-
construction of enzyme mutants MBP-RadAC46, MBP-Arg-RadA, MBP-Glu-RadA, MBP-Asn-RadA, MBP-Pro-RadA, MBP-Asp-RadA, MBP-Ser-RadA, MBP-Cys-RadA, MBP-Gly-RadA, MBP-Arg-RadADELTAC46, MBP-Glu-RadADELTAC46, MBP-Asn-RadADELTAC46, MBP-Pro-RadADELTAC46, MBP-Asp-RadADELTAC46, MBP-Ser-RadADELTAC46, MBP-Cys-RadADELTAC46, and MBP-Gly-RadADELTAC46
-
additional information
-
isolation of the C-terminal ATPase domain by removing the N-terminal domain and the linker that contains the FxxA oligomerisation sequence. To facilitate crystallisation, the unstructured L2 DNA-binding loop is also removed, creating a construct denoted as RadA-ct, analysis of structures of RadA-ct bound to ATP, ADP, AMPPNP and GTP, cyrstal structure of phosphate-bound RadA-ct, overview
-
additional information
-
structure-based rational design of a functional minimized RadA intein with mutation C1A/T1A (intein/extein) and residues 121-130 removed, the structure of the minimized RadA intein reveals the precise interactions between N-extein and the intein, overview. Effects at the -1 position of N-extein and significant improvement of the splicing efficiency of a less robust splicing variant by eliminating the unfavorable extein-intein interactions observed in the structure. Construction of mutant PhoRad Intein harboring the C1A mutation in the intein and a two-residue C-extein with a mutation of Thr to Ala (T+1A), aimed at prevention of splicing and cleavage
-
additional information
-
construction of enzyme mutants MBP-RadAC46, MBP-Arg-RadA, MBP-Glu-RadA, MBP-Asn-RadA, MBP-Pro-RadA, MBP-Asp-RadA, MBP-Ser-RadA, MBP-Cys-RadA, MBP-Gly-RadA, MBP-Arg-RadADELTAC46, MBP-Glu-RadADELTAC46, MBP-Asn-RadADELTAC46, MBP-Pro-RadADELTAC46, MBP-Asp-RadADELTAC46, MBP-Ser-RadADELTAC46, MBP-Cys-RadADELTAC46, and MBP-Gly-RadADELTAC46
-
additional information
-
isolation of the C-terminal ATPase domain by removing the N-terminal domain and the linker that contains the FxxA oligomerisation sequence. To facilitate crystallisation, the unstructured L2 DNA-binding loop is also removed, creating a construct denoted as RadA-ct, analysis of structures of RadA-ct bound to ATP, ADP, AMPPNP and GTP, cyrstal structure of phosphate-bound RadA-ct, overview
-
additional information
-
construction of enzyme mutants MBP-RadAC46, MBP-Arg-RadA, MBP-Glu-RadA, MBP-Asn-RadA, MBP-Pro-RadA, MBP-Asp-RadA, MBP-Ser-RadA, MBP-Cys-RadA, MBP-Gly-RadA, MBP-Arg-RadADELTAC46, MBP-Glu-RadADELTAC46, MBP-Asn-RadADELTAC46, MBP-Pro-RadADELTAC46, MBP-Asp-RadADELTAC46, MBP-Ser-RadADELTAC46, MBP-Cys-RadADELTAC46, and MBP-Gly-RadADELTAC46
-
additional information
-
isolation of the C-terminal ATPase domain by removing the N-terminal domain and the linker that contains the FxxA oligomerisation sequence. To facilitate crystallisation, the unstructured L2 DNA-binding loop is also removed, creating a construct denoted as RadA-ct, analysis of structures of RadA-ct bound to ATP, ADP, AMPPNP and GTP, cyrstal structure of phosphate-bound RadA-ct, overview
-
additional information
-
construction of enzyme mutants MBP-RadAC46, MBP-Arg-RadA, MBP-Glu-RadA, MBP-Asn-RadA, MBP-Pro-RadA, MBP-Asp-RadA, MBP-Ser-RadA, MBP-Cys-RadA, MBP-Gly-RadA, MBP-Arg-RadADELTAC46, MBP-Glu-RadADELTAC46, MBP-Asn-RadADELTAC46, MBP-Pro-RadADELTAC46, MBP-Asp-RadADELTAC46, MBP-Ser-RadADELTAC46, MBP-Cys-RadADELTAC46, and MBP-Gly-RadADELTAC46
-
additional information
-
isolation of the C-terminal ATPase domain by removing the N-terminal domain and the linker that contains the FxxA oligomerisation sequence. To facilitate crystallisation, the unstructured L2 DNA-binding loop is also removed, creating a construct denoted as RadA-ct, analysis of structures of RadA-ct bound to ATP, ADP, AMPPNP and GTP, cyrstal structure of phosphate-bound RadA-ct, overview
-
additional information
-
construction of enzyme mutants MBP-RadAC46, MBP-Arg-RadA, MBP-Glu-RadA, MBP-Asn-RadA, MBP-Pro-RadA, MBP-Asp-RadA, MBP-Ser-RadA, MBP-Cys-RadA, MBP-Gly-RadA, MBP-Arg-RadADELTAC46, MBP-Glu-RadADELTAC46, MBP-Asn-RadADELTAC46, MBP-Pro-RadADELTAC46, MBP-Asp-RadADELTAC46, MBP-Ser-RadADELTAC46, MBP-Cys-RadADELTAC46, and MBP-Gly-RadADELTAC46
-
additional information
-
isolation of the C-terminal ATPase domain by removing the N-terminal domain and the linker that contains the FxxA oligomerisation sequence. To facilitate crystallisation, the unstructured L2 DNA-binding loop is also removed, creating a construct denoted as RadA-ct, analysis of structures of RadA-ct bound to ATP, ADP, AMPPNP and GTP, cyrstal structure of phosphate-bound RadA-ct, overview
-
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Graham, W.J.; Haseltine, C.A.
A recombinase paralog from the hyperthermophilic crenarchaeon Sulfolobus solfataricus enhances SsoRadA ssDNA binding and strand displacement
Gene
515
128-139
2013
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q55075)
brenda
McIlwraith, M.J.; Hall, D.R.; Stasiak, A.Z.; Stasiak, A.; Wigley, D.B.; West, S.C.
RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination
Nucleic Acids Res.
29
4509-4517
2001
Archaeoglobus fulgidus (O29269), Archaeoglobus fulgidus
brenda
Li, Y.; He, Y.; Luo Y.
Conservation of a conformational switch in RadA recombinase from Methanococcus maripaludis
Acta Crystallogr. Sect. D
65
602-610
2009
Methanococcus maripaludis (P0CW58), Methanococcus maripaludis
brenda
Du, L.; Luo, Y.
Structure of a hexameric form of RadA recombinase from Methanococcus voltae
Acta Crystallogr. Sect. F
68
511-516
2012
Methanococcus voltae (O73948), Methanococcus voltae
brenda
Lee, M.H.; Leng, C.H.; Chang, Y.C.; Chou, C.C.; Chen, Y.K.; Hsu, F.F.; Chang, C.S.; Wang, A.H., Wang, T.F.
Self-polymerization of archaeal RadA protein into long and fine helical filaments
Biochem. Biophys. Res. Commun.
323
845-851
2004
Saccharolobus solfataricus
brenda
Qian, X.; Wu, Y.; He, Y.; Luo, Y.
Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change
Biochemistry
44
13753-13761
2005
Methanococcus voltae (O73948), Methanococcus voltae
brenda
Qian, X.; He, Y.; Luo, Y.
Binding of a second magnesium is required for ATPase activity of RadA from Methanococcus voltae
Biochemistry
46
5855-5863
2007
Methanococcus voltae (O73948), Methanococcus voltae
brenda
Graham, W.J. 5th; Rolfsmeier, M.L.; Haseltine, C.A.
An archaeal RadA paralog influences presynaptic filament formation
DNA Repair
12
403-413
2013
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q55075)
brenda
Spies, M.; Kil, Y.; Masui, R.; Kato, R.; Kujo, C.; Ohshima, T.; Kuramitsu, S.; Lanzov, V.
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75C
Eur. J. Biochem.
267
1125-1137
2000
Pyrobaculum islandicum (Q9UWR5), Pyrobaculum islandicum, Pyrobaculum islandicum DSM 4184 (Q9UWR5)
brenda
Seitz, E.M.; Brockman, J.P.; Sandler, S.J.; Clark, A.J.; Kowalczykowski, S.C.
RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
Genes Dev.
12
1248-1253
1998
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q55075)
brenda
Kil, Y.V.; Baitin, D.M.; Masui, R.; Bonch-Osmolovskaya, E.A.; Kuramitsu, S.; Lanzov, V.A.
Efficient strand transfer by the RadA recombinase from the hyperthermophilic archaeon Desulfurococcus amylolyticus
J. Bacteriol.
182
130-134
2000
Desulfurococcus amylolyticus (Q9Y8J4), Desulfurococcus amylolyticus
brenda
Kil, Y.V.; Glazunov, E.A.; Lanzov, V.A.
Characteristic thermodependence of the RadA recombinase from the hyperthermophilic archaeon Desulfurococcus amylolyticus
J. Bacteriol.
187
2555-2557
2005
Desulfurococcus amylolyticus (Q9Y8J4), Desulfurococcus amylolyticus
brenda
Komori, K.; Miyata, T.; DiRuggiero, J.; Holley-Shanks, R.; Hayashi, I.; Cann, I.K.; Mayanagi, K.; Shinagawa, H.; Ishino, Y.
Both RadA and RadB are involved in homologous recombination in Pyrococcus furiosus
J. Biol. Chem.
275
33782-33790
2000
Pyrococcus furiosus (O74036), Pyrococcus furiosus
brenda
Komori, K.; Miyata, T.; Daiyasu, H.; Toh, H.; Shinagawa, H.; Ishino, aY.
Domain analysis of an archaeal RadA protein for the strand exchange activity
J. Biol. Chem.
275
33791-33797
2000
Pyrococcus furiosus (O74036), Pyrococcus furiosus
brenda
Komori, K.; Ishino, Y.
Replication protein A in Pyrococcus furiosus is involved in homologous DNA recombination
J. Biol. Chem.
276
25654-25660
2001
Pyrococcus furiosus
brenda
Qian, X.; He, Y.; Wu, Y.; Luo, Y.
Asp302 determines potassium dependence of a RadA recombinase from Methanococcus voltae
J. Mol. Biol.
360
537-547
2006
Methanococcus voltae (O73948), Methanococcus voltae
brenda
Rolfsmeier, M.L.; Haseltine, C.A.
The single-stranded DNA binding protein of Sulfolobus solfataricus acts in the presynaptic step of homologous recombination
J. Mol. Biol.
397
31-45
2010
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus
brenda
Wu, Y.; He, Y.; Moya, I.A.; Qian, X.; Luo, Y.
Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation
Mol. Cell.
15
423-435
2004
Methanococcus voltae (O73948), Methanococcus voltae
brenda
Seitz, E.M.; Kowalczykowski, S.C.
The DNA binding and pairing preferences of the archaeal RadA protein demonstrate a universal characteristic of DNA strand exchange proteins
Mol. Microbiol.
37
555-560
2000
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q55075)
brenda
Ariza, A.; Richard, D.J.; White, M.F.; Bond, C.S.
Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA
Nucleic Acids Res.
33
1465-1473
2005
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q55075)
brenda
Chen, L.T.; Ko, T.P.; Chang, Y.C.; Lin, K.A.; Chang, C.S.; Wang, A.H.; Wang, T.F.
Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
Nucleic Acids Res.
35
1787-1801
2007
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus P2 (Q55075)
brenda
Haseltine, C.A.; Kowalczykowski, S.C.
An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA
Nucleic Acids Res.
37
2757-2770
2009
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus
brenda
Chen, L.T.; Ko, T.P.; Chang, Y.W.; Lin, K.A.; Wang, A.H.; Wang, T.F.
Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein
PLoS One
2
e858
2007
Saccharolobus solfataricus (Q55075)
brenda
Zhang, C.; Tian, B.; Li, S.; Ao, X.; Dalgaard, K.; Goekce, S.; Liang, Y.; She, Q.
Genetic manipulation in Sulfolobus islandicus and functional analysis of DNA repair genes
Biochem. Soc. Trans.
41
405-410
2013
Sulfolobus islandicus
brenda
Han, W.; Shen, Y.; She, Q.
Nanobiomotors of archaeal DNA repair machineries: current research status and application potential
Cell Biosci.
4
32
2014
Archaeoglobus fulgidus, Sulfolobus islandicus, Sulfurisphaera tokodaii, Methanococcus voltae (O73948), Pyrococcus furiosus (O74036), Saccharolobus solfataricus (Q55075), Thermoplasma acidophilum (Q9HJ68), Saccharolobus solfataricus P2 (Q55075), Thermoplasma acidophilum ATCC 25905 (Q9HJ68)
brenda
Flores, G.E.; Wagner, I.D.; Liu, Y.; Reysenbach, A.L.
Distribution, abundance, and diversity patterns of the thermoacidophilic deep-sea hydrothermal vent euryarchaeota 2
Front. Microbiol.
3
47
2012
Aciduliprofundum boonei, Aciduliprofundum boonei T469
brenda
Stefanska, A.; Gaffke, L.; Kaczorowska, A.K.; Plotka, M.; Dabrowski, S.; Kaczorowski, T.
Highly thermostable RadA protein from the archaeon Pyrococcus woesei enhances specificity of simplex and multiplex PCR assays
J. Appl. Genet.
57
239-249
2016
Pyrococcus woesei (A0A0D3MA54), Pyrococcus woesei DSM 3773 (A0A0D3MA54)
brenda
Oeemig, J.S.; Zhou, D.; Kajander, T.; Wlodawer, A.; Iwai, H.
NMR and crystal structures of the Pyrococcus horikoshii RadA intein guide a strategy for engineering a highly efficient and promiscuous intein
J. Mol. Biol.
421
85-99
2012
Pyrococcus horikoshii (O58001), Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860 (O58001)
brenda
Wang, L.; Sheng, D.; Han, W.; Huang, B.; Zhu, S.; Ni, J.; Li, J.; Shen, Y.
Sulfolobus tokodaii RadA paralog, stRadC2, is involved in DNA recombination via interaction with RadA and Hjc
Sci. China Life Sci.
55
261-267
2012
Sulfurisphaera tokodaii (Q975Y1), Sulfurisphaera tokodaii
brenda
Liu, J.; Ekanayake, O.; Santoleri, D.; Walker, K.; Rozovsky, S.
Efficient generation of hydrazides in proteins by RadA split intein
ChemBioChem
20
1-8
2019
Pyrococcus horikoshii (O58001), Pyrococcus horikoshii DSM 12428 (O58001), Pyrococcus horikoshii NBRC 100139 (O58001), Pyrococcus horikoshii JCM 9974 (O58001), Pyrococcus horikoshii ATCC 700860 (O58001), Pyrococcus horikoshii OT-3 (O58001)
brenda
Cooper, D.; Lovett, S.
Recombinational branch migration by the RadA/Sms paralog of RecA in Escherichia coli
eLife
5
e10807
2016
Escherichia coli (P24554), Escherichia coli
brenda
Marsh, M.E.; Scott, D.E.; Ehebauer, M.T.; Abell, C.; Blundell, T.L.; Hyvoenen, M.
ATP half-sites in RadA and RAD51 recombinases bind nucleotides
FEBS open bio
6
372-385
2016
Homo sapiens, Pyrococcus horikoshii (O58001), Pyrococcus horikoshii DSM 12428 (O58001), Pyrococcus horikoshii NBRC 100139 (O58001), Pyrococcus horikoshii JCM 9974 (O58001), Pyrococcus horikoshii ATCC 700860 (O58001), Pyrococcus horikoshii OT-3 (O58001)
brenda
Rolfsmeier, M.; Haseltine, C.
The RadA recombinase and paralogs of the hyperthermophilic archaeon Sulfolobus solfataricus
Methods Enzymol.
600
255-284
2018
Saccharolobus solfataricus (Q55075), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q55075), Saccharolobus solfataricus JCM 11322 (Q55075), Saccharolobus solfataricus ATCC 35092 (Q55075), Saccharolobus solfataricus DSM 1617 (Q55075)
brenda
Patoli, B.B.; Winter, J.A.; Patoli, A.A.; Delahay, R.M.; Bunting, K.A.
Co-expression and purification of the RadA recombinase with the RadB paralog from Haloferax volcanii yields heteromeric ring-like structures
Microbiology
163
1802-1811
2017
Haloferax volcanii (Q48328), Haloferax volcanii, Haloferax volcanii NCIMB 2012 (Q48328), Haloferax volcanii JCM 8879 (Q48328), Haloferax volcanii DS2 (Q48328), Haloferax volcanii DSM 3757 (Q48328), Haloferax volcanii ATCC 29605 (Q48328), Haloferax volcanii NBRC 14742 (Q48328), Haloferax volcanii VKM B-1768 (Q48328)
brenda
Mason, J.M.; Dusad, K.; Wright, W.D.; Grubb, J.; Budke, B.; Heyer, W.D.; Connell, P.P.; Weichselbaum, R.R.; Bishop, D.K.
RAD54 family translocases counter genotoxic effects of RAD51 in human tumor cells
Nucleic Acids Res.
43
3180-3196
2015
Homo sapiens (Q06609), Homo sapiens
brenda
Topilina, N.I.; Novikova, O.; Stanger, M.; Banavali, N.K.; Belfort, M.
Post-translational environmental switch of RadA activity by extein-intein interactions in protein splicing
Nucleic Acids Res.
43
6631-6648
2015
Pyrococcus horikoshii (O58001), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58001)
brenda
Torres, R.; Serrano, E.; Alonso, J.
Bacillus subtilis RecA interacts with and loads RadA/Sms to unwind recombination intermediates during natural chromosomal transformation
Nucleic Acids Res.
47
9198-9215
2019
Bacillus subtilis (P37572), Bacillus subtilis, Bacillus subtilis 168 (P37572)
brenda