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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 |
2000-11-3
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pubmed:abstractText |
Rad51 and Rad54 proteins are important for the repair of double-stranded DNA (dsDNA) breaks by homologous recombination in eukaryotes. Rad51 assembles on single-stranded DNA (ssDNA) to form a helical nucleoprotein filament that performs homologous pairing with dsDNA; Rad54 stimulates this pairing substantially. Here, we demonstrate that Rad54 acts in concert with the mature Rad51-ssDNA filament. Enhancement of DNA pairing by Rad54 is greatest at an equimolar ratio relative to Rad51 within the filament. Reciprocally, the Rad51-ssDNA filament enhances both the dsDNA-dependent ATPase and the dsDNA unwinding activities of Rad54. We conclude that Rad54 participates in the DNA homology search as a component of the Rad51-nucleoprotein filament and that the filament delivers Rad54 to the dsDNA pairing locus, thereby linking the unwinding of potential target DNA with the homology search process.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Superhelical,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAD51 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD51 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RAD54 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Rad51 Recombinase,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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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 |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
583-92
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11030338-Adenosine Triphosphatases,
pubmed-meshheading:11030338-Cell Nucleus,
pubmed-meshheading:11030338-DNA, Single-Stranded,
pubmed-meshheading:11030338-DNA, Superhelical,
pubmed-meshheading:11030338-DNA Helicases,
pubmed-meshheading:11030338-DNA Repair,
pubmed-meshheading:11030338-DNA Repair Enzymes,
pubmed-meshheading:11030338-DNA-Binding Proteins,
pubmed-meshheading:11030338-Escherichia coli,
pubmed-meshheading:11030338-Fungal Proteins,
pubmed-meshheading:11030338-Humans,
pubmed-meshheading:11030338-Rad51 Recombinase,
pubmed-meshheading:11030338-Saccharomyces cerevisiae,
pubmed-meshheading:11030338-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11030338-Species Specificity
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pubmed:year |
2000
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pubmed:articleTitle |
Rad54 protein is targeted to pairing loci by the Rad51 nucleoprotein filament.
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pubmed:affiliation |
Division of Biological Sciences, University of California, Davis 95616, 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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