DNA nicking by Escherichia coli topoisomerase IV with a substitution mutation from tyrosine to histidine at the active site.

doi:10.1046/j.1365-2443.1996.d01-226.x

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Article

DNA nicking by Escherichia coli topoisomerase IV with a substitution mutation from tyrosine to histidine at the active site.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Dec 1996

Yokochi T, Kato J, Ikeda H

Abstract excerpt

BACKGROUND: Escherichia coli topoisomerase IV is a type II topoisomerase composed of ParC and ParE subunits and plays a major role in the decatenation of replicated molecules. The reaction with type II topoisomerases involves the cutting through transesterification between an active-site tyrosine and a DNA phosphodiester bond and a rejoining of cleaved DNA. RESULTS: To genetically analyse the mechanism of this...

Topics

Base Sequence
Binding Sites
DNA
DNA Topoisomerases, Type II
Escherichia coli
Histidine
Mutation
Tyrosine

Source

Open in PubMed

Identifiers

PMID: 9077455
DOI: 10.1046/j.1365-2443.1996.d01-226.x

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