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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2003-10-6
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pubmed:abstractText |
Functional 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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase I,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eme1protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Endonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/MUS81 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/xeroderma pigmentosum group F...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
747-59
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14527419-Cells, Cultured,
pubmed-meshheading:14527419-DNA,
pubmed-meshheading:14527419-DNA Polymerase I,
pubmed-meshheading:14527419-DNA Replication,
pubmed-meshheading:14527419-DNA-Binding Proteins,
pubmed-meshheading:14527419-Endonucleases,
pubmed-meshheading:14527419-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:14527419-Gene Expression Regulation, Fungal,
pubmed-meshheading:14527419-Macromolecular Substances,
pubmed-meshheading:14527419-Mutation,
pubmed-meshheading:14527419-Nucleic Acid Conformation,
pubmed-meshheading:14527419-Proteins,
pubmed-meshheading:14527419-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:14527419-Schizosaccharomyces,
pubmed-meshheading:14527419-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:14527419-Substrate Specificity
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pubmed:year |
2003
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pubmed:articleTitle |
The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick and counternick mechanism.
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pubmed:affiliation |
Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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