Linked Life Data

14527419

Source:http://linkedlifedata.com/resource/pubmed/id/14527419

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pubmed-article:14527419pubmed:abstractTextFunctional studies strongly suggest that the Mus81-Eme1 complex resolves Holliday junctions (HJs) in fission yeast, but in vitro it preferentially cleaves flexible three-way branched structures that model replication forks or 3' flaps. Here we report that a nicked HJ is the preferred substrate of endogenous and recombinant Mus81-Eme1. Cleavage occurs specifically on the strand that opposes the nick, resulting in resolution of the structure into linear duplex products. Resolving cuts made by the endogenous Mus81-Eme1 complex on an intact HJ are quasi-simultaneous, indicating that Mus81-Eme1 resolves HJs by a nick and counternick mechanism, with a large rate enhancement of the second cut arising from the flexible nature of the nicked HJ intermediate. Recombinant Mus81-Eme1 is ineffective at making the first cut. We also report that HJs accumulate in a DNA polymerase alpha mutant that lacks Mus81, providing further evidence that the Mus81-Eme1 complex targets HJs in vivo.lld:pubmed
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pubmed-article:14527419pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:14527419pubmed:articleTitleThe endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick and counternick mechanism.lld:pubmed
pubmed-article:14527419pubmed:affiliationDepartment of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.lld:pubmed
pubmed-article:14527419pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14527419pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:14527419pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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