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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5103
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pubmed:dateCreated |
1993-4-22
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pubmed:abstractText |
The RAD51 protein functions in the processes of DNA repair and in mitotic and meiotic genetic recombination in the yeast Saccharomyces cerevisiae. The protein has adenosine triphosphate-dependent DNA binding activities similar to those of the Escherichia coli RecA protein, and the two proteins have 30 percent sequence homology. RAD51 polymerized on double-stranded DNA to form a helical filament nearly identical in low-resolution, three-dimensional structure to that formed by RecA. Like RecA, RAD51 also appears to force DNA into a conformation of approximately a 5.1-angstrom rise per base pair and 18.6 base pairs per turn. As in other protein families, its structural conservation appears to be stronger than its sequence conservation. Both the structure of the protein polymer formed by RecA and the DNA conformation induced by RecA appear to be general properties of a class of recombination proteins found in prokaryotes as well as eukaryotes.
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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 Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
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 Recombinase,
http://linkedlifedata.com/resource/pubmed/chemical/Rec A Recombinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1896-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8456314-Adenosine Triphosphate,
pubmed-meshheading:8456314-Binding Sites,
pubmed-meshheading:8456314-DNA,
pubmed-meshheading:8456314-DNA, Single-Stranded,
pubmed-meshheading:8456314-DNA Repair,
pubmed-meshheading:8456314-DNA-Binding Proteins,
pubmed-meshheading:8456314-Fourier Analysis,
pubmed-meshheading:8456314-Fungal Proteins,
pubmed-meshheading:8456314-Meiosis,
pubmed-meshheading:8456314-Mitosis,
pubmed-meshheading:8456314-Molecular Structure,
pubmed-meshheading:8456314-Nucleic Acid Conformation,
pubmed-meshheading:8456314-Protein Structure, Secondary,
pubmed-meshheading:8456314-Rad51 Recombinase,
pubmed-meshheading:8456314-Rec A Recombinases,
pubmed-meshheading:8456314-Recombinant Proteins,
pubmed-meshheading:8456314-Saccharomyces cerevisiae,
pubmed-meshheading:8456314-Saccharomyces cerevisiae Proteins
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pubmed:year |
1993
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pubmed:articleTitle |
Similarity of the yeast RAD51 filament to the bacterial RecA filament.
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pubmed:affiliation |
Department of Biology, Osaka University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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