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

Zhiyu Li, Alfonso Mondragón, Hiroshi Hiasa, Kenneth J. Marians, Russell J. DiGate*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)888-895
Number of pages8
JournalMolecular Microbiology
Volume35
Issue number4
DOIs
StatePublished - 2000

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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