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

doi:10.1046/j.1365-2958.2000.01763.x

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

Pharmacology

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40 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 language	English (US)
Pages (from-to)	888-895
Number of pages	8
Journal	Molecular Microbiology
Volume	35
Issue number	4
DOIs	https://doi.org/10.1046/j.1365-2958.2000.01763.x
State	Published - 2000

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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.",

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T1 - Identification of a unique domain essential for Escherichia coli DNA topoisomerase III-catalysed decatenation of replication intermediates

AU - Li, Zhiyu

AU - Mondragón, Alfonso

AU - Hiasa, Hiroshi

AU - Marians, Kenneth J.

AU - DiGate, Russell J.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

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DO - 10.1046/j.1365-2958.2000.01763.x

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

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