Source:http://linkedlifedata.com/resource/pubmed/id/15686518
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2005-2-2
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pubmed:abstractText |
In addition to the recombinase Rad51, vertebrates have five paralogs of Rad51, all members of the Rad51-dependent recombination pathway. These paralogs form two complexes (Rad51C/Xrcc3 and Rad51B/C/D/Xrcc2), which play roles in somatic recombination, DNA repair and chromosome stability. However, little is known of their possible involvement in meiosis, due to the inviability of the corresponding knockout mice. We have recently reported that the Arabidopsis homolog of one of these Rad51 paralogs (AtXrcc3) is involved in DNA repair and meiotic recombination and present here Arabidopsis lines carrying mutations in three other Rad51 paralogs (AtRad51B, AtRad51C and AtXrcc2). Disruption of any one of these paralogs confers hypersensitivity to the DNA cross-linking agent Mitomycin C, but not to gamma-irradiation. Moreover, the atrad51c-1 mutant is the only one of these to show meiotic defects similar to those of the atxrcc3 mutant, and thus only the Rad51C/Xrcc3 complex is required to achieve meiosis. These results support conservation of functions of the Rad51 paralogs between vertebrates and plants and differing requirements for the Rad51 paralogs in meiosis and DNA repair.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATRAD51 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitomycin,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Rad51 Recombinase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0960-7412
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
533-45
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15686518-Amino Acid Sequence,
pubmed-meshheading:15686518-Arabidopsis,
pubmed-meshheading:15686518-Arabidopsis Proteins,
pubmed-meshheading:15686518-Cross-Linking Reagents,
pubmed-meshheading:15686518-DNA Repair,
pubmed-meshheading:15686518-DNA-Binding Proteins,
pubmed-meshheading:15686518-Gamma Rays,
pubmed-meshheading:15686518-Infertility,
pubmed-meshheading:15686518-Meiosis,
pubmed-meshheading:15686518-Mitomycin,
pubmed-meshheading:15686518-Molecular Sequence Data,
pubmed-meshheading:15686518-Mutation,
pubmed-meshheading:15686518-Phenotype,
pubmed-meshheading:15686518-Phylogeny,
pubmed-meshheading:15686518-Protein Isoforms,
pubmed-meshheading:15686518-Rad51 Recombinase,
pubmed-meshheading:15686518-Sequence Homology, Amino Acid
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pubmed:year |
2005
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pubmed:articleTitle |
Differing requirements for the Arabidopsis Rad51 paralogs in meiosis and DNA repair.
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pubmed:affiliation |
CNRS UMR6547, Université Blaise Pascal, 24, avenue des Landais, 63177 Aubière, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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