Are two better than one? Analysis of an FtsK/Xer recombination system that uses a single recombinase
Bacteria harbouring circular chromosomes have a Xer site-specific recombination system that resolves chromosome dimers at division. In Escherichia coli, the activity of the XerCD/dif system is controlled and coupled with cell division by the FtsK DNA translocase. Most Xer systems, as XerCD/dif, incl...
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Published in | Nucleic acids research Vol. 38; no. 19; pp. 6477 - 6489 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
Oxford University Press
01.10.2010
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Subjects | |
Online Access | Get full text |
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Summary: | Bacteria harbouring circular chromosomes have a Xer site-specific recombination system that resolves chromosome dimers at division. In Escherichia coli, the activity of the XerCD/dif system is controlled and coupled with cell division by the FtsK DNA translocase. Most Xer systems, as XerCD/dif, include two different recombinases. However, some, as the Lactococcus lactis XerS/difSL system, include only one recombinase. We investigated the functional effects of this difference by studying the XerS/difSL system. XerS bound and recombined difSL sites in vitro, both activities displaying asymmetric characteristics. Resolution of chromosome dimers by XerS/difSL required translocation by division septum-borne FtsK. The translocase domain of L. lactis FtsK supported recombination by XerCD/dif, just as E. coli FtsK supports recombination by XerS/difSL. Thus, the FtsK-dependent coupling of chromosome segregation with cell division extends to non-rod-shaped bacteria and outside the phylum Proteobacteria. Both the XerCD/dif and XerS/difSL recombination systems require the control activities of the FtsKγ subdomain. However, FtsKγ activates recombination through different mechanisms in these two Xer systems. We show that FtsKγ alone activates XerCD/dif recombination. In contrast, both FtsKγ and the translocation motor are required to activate XerS/difSL recombination. These findings have implications for the mechanisms by which FtsK activates recombination. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
ISSN: | 0305-1048 1362-4962 1362-4962 |
DOI: | 10.1093/nar/gkq507 |