Polymerization of SopA partition ATPase: regulation by DNA binding and SopB

In bacteria, mitotic stability of plasmids and many chromosomes depends on replicon-specific systems which comprise a centromere, a centromere-binding protein and an ATPase. Dynamic self-assembly of the ATPase appears to enable active partition of replicon copies into cell-halves, but for most ATPas...

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Published inMolecular microbiology Vol. 63; no. 2; pp. 468 - 481
Main Authors Bouet, Jean-Yves, Ah-Seng, Yoan, Benmeradi, Nacer, Lane, David
Format Journal Article
LanguageEnglish
Published Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.01.2007
Blackwell Publishing Ltd
Blackwell Science
Wiley
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Summary:In bacteria, mitotic stability of plasmids and many chromosomes depends on replicon-specific systems which comprise a centromere, a centromere-binding protein and an ATPase. Dynamic self-assembly of the ATPase appears to enable active partition of replicon copies into cell-halves, but for most ATPases (the Walker-box type) the mechanism is unknown. Also unknown is how the host cell contributes to partition. We have examined the effects of non-sequence-specific DNA on in vitro self-assembly of the SopA partition ATPase of plasmid F. SopA underwent polymerization provided ATP was present. DNA inhibited this polymerization and caused breakdown of pre-formed polymers. Centromere-binding protein SopB counteracted DNA-mediated inhibition by itself binding to and masking the DNA, as well as by stimulating polymerization directly. The results suggest that in vivo, SopB smothers DNA by spreading from sopC, allowing SopA-ATP polymerization which initiates plasmid displacement. We propose that SopB and nucleoid DNA regulate SopA polymerization and hence partition.
Bibliography:http://dx.doi.org/10.1111/j.1365-2958.2006.05537.x
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ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2006.05537.x