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heterotetramer
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silver staining, Western blotting, cross-linking of topo IV with glutaraldehyde in the absence of DNA. Southern blotting, cross-linking of Topo IV in the presence of DNA, composed of two molecules each of ParC and ParE, topo IV binds the gate segment and the transport segment of DNA. The Par E subunit dimerize prior to strand passage
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Drosophila sp. (in: flies)
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x * 135000, SDS-PAGE
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peptides with topoisomerase I activity detected by SDS-PAGE: 105000 MW, 83000 MW, 54000 MW and 30000 MW
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x * 71500, SDS-PAGE
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x * 99353, calculation from nucleotide sequence
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x * 99353, calculation from nucleotide sequence
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x * 30000, SDS-PAGE, may exist as a multimeric protein in the native state
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proteins with MW 75000, 83000, 91000 or 100000 with DNA topoisomerase I activity are detected
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x * 76000, SDS-PAGE
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x * 90000 + x * 36000, the large subunit contains the DNA-binding domain, the small subunit contains the catalytic domain, each subunit is essential for trypanosome survival
dimer
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2 * 100000, SDS-PAGE. DNA topoisomerase I exists largely in a monomeric form, but also has a minor population of the dimeric form
dimer
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1 * 29000 + 1 * 73000, LdTOP1L (large subunit) and LdTOP1S (small subunit) form a direct 1:1 heterodimer complex through protein-protein interaction, SDS-PAGE
heterodimer
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DNA topoisomerase I of kinetoplastid protozoan parasite Leishmania donovani is an unusual bi-subunit enzyme. To find out the differential affinity of 3,3-diindolylmethane towards the large subunit (LdTOP1L) and small subunit (LdTOP1S) of Leishmania donovani topoisomerase I, performed the binding of individual subunits with 3,3-diindolylmethane by equilibrium dialysis experiment
heterodimer
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Leishmania donovani topoisomerase I is an unusual bi-subunit enzyme where the core DNA binding domain and the catalytic domain harboring the consensus SKXXY motif lie in separate subunits. The two subunits (LdTOP1L and LdTOP1S) are synthesized by two different genes, which associate with each other through proteinprotein interaction to form an active heterodimeric topoisomerase I within the parasite
heterodimer
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the genes encoding each protein subunit are located on different chromosomes
heterodimer
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unique heterodimeric DNA topoisomerase IB, consists of a large subunit (LdTop1L), which contains the non-conserved N-terminal end and a phylogenetically conserved core domain, and of a small subunit (LdTop1S) which harbours the C-terminal region with a characteristic tyrosine residue in the active site
heterodimer
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large subunit (LdTOPIL or L) and the catalytic small subunit (LdTOPIS or S)
heterodimer
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presence of two separate genes encoding for the core and catalytic domains, indicating that this singular feature is common to all trypanosomatids
monomer
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The sedimentation results are consistent with MimiTopIB being a monomer in solution, although the prospect that MimiTopIB is an asymmetrically shaped homodimer cannot excluded
monomer
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1 * 63000, SDS-PAGE. The purified 63000 MW protein is a proteolytic fragment of a protein with a molecular mass of 100000
monomer
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1 * 80000, SDS-PAGE
monomer
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1 * 79000, SDS-PAGE
monomer
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1 * 108000, electrophoresis under denaturing conditions
monomer
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1 * 108000, electrophoresis under denaturing conditions
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monomer
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1 * 110000, denaturing PAGE
monomer
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1 * 62000, SDS-PAGE
monomer
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1 * 100000, SDS-PAGE
monomer
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1 * 100000, SDS-PAGE. DNA topoisomerase I exists largely in a monomeric form, but also has a minor population of the dimeric form
monomer
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765 amino acids. All type IB topoisomerases contain a conserved SKXXY signature in the region in which a tyrosine residue (Tyr-723 in the human topoisomeraseI) is the DNA-cleaving amino acid
monomer
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usually works as a monomer, previously shown that two molecules can form a dimer-like protein-protein complex on a suicide DNA substrate resulting in a topoisomerase I double cleavage complex. Here human topoisomerase I forms a transient dimer. Probably human topoisomerase I double cleavage complexes are part of the normal catalytic cycle of this enzyme that occur in vitro and possibly also in vivo
monomer
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the kinetoplastid family (Trypanosoma and Leishmania) possess an unusual bisubunit topoisomerase I. In vitro gene fusion of Leishmania bisubunit topoisomerase I into a single ORF encoding a new monomeric topoisomerase I (LdTOPIL-fus-S). This unusual structure of DNA topoisomerase I may provide a missing link in the evolution of type IB enzymes. LdTOPIL-fus-S fusion protein is a functional topoisomerase I. DNA-binding assays shown
monomer
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765 amino acids. All type IB topoisomerases contain a conserved SKXXY signature in the regionin which a tyrosine residue is the DNA-cleaving amino acid
monomer
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1 * 98000, enzyme form p98, SDS-PAGE. The two enzyme form P98 and p102 are structurally related
monomer
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1 * 102000, enzyme form p102, SDS-PAGE. The two enzyme forms P98 and p102 are structurally related
monomer
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Three structural domains, N-terminus domain (134 amino acids) poorly conserved, a 500 amino acid length block of conserved amino acids with high homology to the core domain of the human protein, the C-terminal domain is smaller than the hosts' but conserves the active tyrosine at position 798 which makes the enzyme fully active
monomer
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1 * 90000, SDS-PAGE
monomer
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1 * 65000, SDS-PAGE
monomer
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1 * 30000, SDS-PAGE
monomer
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1 * 33000, SDS-PAGE
additional information
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the DraTopIB 139GSDIYARQHK148 peptide forms a well-ordered alpha-helix that mimics the specificity helix of poxvirus TopIB, comparison of structures of DraTopIB and poxvirus TopIB, overview. Several mechanisms might exist to trigger the folding of the specificity heli
additional information
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other cross-linking reagents than glutaraldehyde tested. Western blot analysis of cross-linked topo IV bound to DNA. Model for topo IV tetramers bound to (-)- and (+)-SC DNA shown
additional information
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the enzyme structure with bound DNA shows distinct conformational changes from the structure of the enzyme without bound DNA, overview. The portion of cleaved DNA 5' to the site of cleavage is anchored tightly with extensive noncovalent protein-DNA interactions. The portion of the oligonucleotide 5' to the cleavage site binds in a deep groove formed at the interface of domains I and III as well as within domain IV, in a similar orientation. Structure comparison of wild-type and D111N mutant enzymes, overview
additional information
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the enzyme contains an N-terminal catalytic fragment of 67 kDa and a C-terminal zinc binding region of 30 kDa
additional information
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TopA contains an N-terminal catalytic fragment and a C-terminal zinc-binding region that is required for relaxation of the negatively supercoiled DNA
additional information
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relaxation activity of human TopI by adding to the core domain a series of peptides containing the C-terminal domain in the presence of DNA. Reinforced by using a two-hybrid expression system, identified proteins containing part of the linker and the C-terminal domain that supplemented the catalytic core of Saccharomyces cerevisiae topoisomerase I
additional information
structure-activity relationship, overview
additional information
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structure-activity relationship study, overview
additional information
structure-function relationship, molecular dynamics modelling, detailed overview. Topo I is a single polypeptide of 765 amino acid residues comprising four domains called: N-terminal domain with residues M1-G214, core domain with I215-A635, linker domain with P636-K712, and C-terminal domain with Q713-F765 domain. The core domain is further divided into three subdomains that form two distinct lobes in the three-dimensional structure of topo I: the cap region, including subdomains I formed by residues I215-E232 and S320-S433, subdomain II formed by residues P233-M319, and the separate subdomain III consisting of residues R434-A635
additional information
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structure-function relationship, molecular dynamics modelling, detailed overview. Topo I is a single polypeptide of 765 amino acid residues comprising four domains called: N-terminal domain with residues M1-G214, core domain with I215-A635, linker domain with P636-K712, and C-terminal domain with Q713-F765 domain. The core domain is further divided into three subdomains that form two distinct lobes in the three-dimensional structure of topo I: the cap region, including subdomains I formed by residues I215-E232 and S320-S433, subdomain II formed by residues P233-M319, and the separate subdomain III consisting of residues R434-A635
additional information
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Topo I is a single polypeptide of 765 amino acid residues composed of four domains: N-terminal domain (residues 1-214), core domain (residues 215-635), linker domain (residues 636-712), and C-terminal domain (residues 713-765). The core domain is further divided into three subdomains that form two distinct lobes in the threedimensional structure of topo I: the cap, including subdomains I and II (residues 215-433), and subdomain III (residues 434-635). Interactions between N-terminal domain and other domains of topo I are different for the protein in a complex with either DNA or SRSF1
additional information
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important role by part of the N-terminal extension of the small subunit of DNA topoisomerase I, contribute with a main portion of the linker domain of this enzyme
additional information
three-dimensional ribbon structure of LdTopIIIbeta generated based on the crystal structure of Escherichia coli topo isomerase III, overview
additional information
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three-dimensional ribbon structure of LdTopIIIbeta generated based on the crystal structure of Escherichia coli topo isomerase III, overview
additional information
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three-dimensional ribbon structure of LdTopIIIbeta generated based on the crystal structure of Escherichia coli topo isomerase III, overview
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additional information
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structure-function analysis of MtTOP1, overview
additional information
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regulation of DNA topoisomerase I, different expression patterns described in the distinct life cycle stages of Plasmodium falciparum. An indirect evidence of potential post-translational mechanisms which could operate on Plasmodium topoisomerases at different stages of its life cycle
additional information
domain mapping analysis shows that the enzyme is composed of conserved four domains, I through IV, together with a variable C-terminal region containing a unique domain V
additional information
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domain mapping analysis shows that the enzyme is composed of conserved four domains, I through IV, together with a variable C-terminal region containing a unique domain V
additional information
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domain mapping analysis shows that the enzyme is composed of conserved four domains, I through IV, together with a variable C-terminal region containing a unique domain V
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additional information
multimeric status of Trypanosoma brucei TopI. Molecular mass determination by gel filtration chromatography suggests that the native enzyme might exist as a tetrameric active A2B2 form or two heterodimers would facilitate the binding at the helical crossover points of DNA
additional information
three-dimensional structure model, overview