Identification of a unique domain essential for Escherichia coli DNA topoisomerase III-catalysed decatenation of replication intermediates Journal Article


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
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  1. Kenneth Marians
    138 Marians
  2. Hiroshi   Hiasa
    21 Hiasa