Authors: | Li, Z.; Mondragón, A.; Hiasa, H.; Marians, K. J.; DiGate, R. J. |
Article Title: | Identification of a unique domain essential for Escherichia coli DNA topoisomerase III-catalysed decatenation of replication intermediates |
Abstract: | A 17-amino-acid residue domain has been identified in Escherichia coli DNA topoisomerase II (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. |
Keywords: | controlled study; nonhuman; dna replication; protein domain; protein binding; bacteria (microorganisms); amino acid sequence; molecular sequence data; sequence homology, amino acid; recombinant fusion proteins; escherichia coli; substrate specificity; dimerization; protein structure, tertiary; binding sites; nucleic acid conformation; dna, bacterial; dna topoisomerase; dna topoisomerases, type i; plasmid dna; dna supercoiling; dna, superhelical; dimer; negibacteria; priority journal; article |
Journal Title: | Molecular Microbiology |
Volume: | 35 |
Issue: | 4 |
ISSN: | 0950-382X |
Publisher: | Blackwell Publishing |
Date Published: | 2000-02-01 |
Start Page: | 888 |
End Page: | 895 |
Language: | English |
DOI: | 10.1046/j.1365-2958.2000.01763.x |
PUBMED: | 10692165 |
PROVIDER: | scopus |
DOI/URL: | |
Notes: | Export Date: 18 November 2015 -- Source: Scopus |