PMID:10692165: Difference between revisions

Revision as of 17:51, 1 September 2013

Citation	No author listed (2000) Identification of a unique domain essential for Escherichia coli DNA topoisomerase III-catalysed decatenation of replication intermediates. Mol. Microbiol. 35:888-95
Abstract	A 17-amino-acid residue domain has been identified in Escherichia coli DNA topoisomerase III (Topo III) that is essential for Topo III-mediated resolution of DNA replication intermediates in vitro. Deletion of this domain reduced Topo III-catalysed resolution of DNA replication intermediates and decatenation of multiply linked plasmid DNA dimers by four orders of magnitude, whereas reducing Topo III-catalysed relaxation of negatively supercoiled DNA substrates only 20-fold. The presence of this domain has been detected in multiple plasmid-encoded topoisomerases, raising the possibility that these enzymes may also be decatenases.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; DNA Replication; DNA Topoisomerases, Type I/chemistry; DNA Topoisomerases, Type I/genetics; DNA Topoisomerases, Type I/metabolism; DNA, Bacterial/genetics; DNA, Bacterial/metabolism; DNA, Superhelical/chemistry; DNA, Superhelical/metabolism; Dimerization; Escherichia coli/enzymology; Escherichia coli/genetics; Molecular Sequence Data; Nucleic Acid Conformation; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Sequence Homology, Amino Acid; Substrate Specificity
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