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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
2003-12-24
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pubmed:databankReference |
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pubmed:abstractText |
Homologous recombination is an important biological process that occurs in all organisms and facilitates genome rearrangements and repair of DNA double-strand breaks. Eukaryotic Rad51 proteins (Rad51sp or Rhp51 in fission yeast) are functional and structural homologs of bacterial RecA protein, an evolutionarily conserved protein that plays a key role in homologous pairing and strand exchange between homologous DNA molecules in vitro. Here we show that the fission yeast swi5+ gene, which was originally identified as a gene required for normal mating-type switching, encodes a protein conserved among eukaryotes and is involved in a previously uncharacterized Rhp51 (Rad51sp)-dependent recombination repair pathway that does not require the Rhp55/57 (Rad55/57sp) function. Protein interactions with both Swi5 and Rhp51 were found to be mediated by a domain common to Swi2 and Sfr1 (Swi five-dependent recombination repair protein 1, a previously uncharacterized protein with sequence similarity to the C-terminal part of Swi2). Genetic epistasis analyses suggest that the Swi5-Sfr1-Rhp51 interactions function specifically in DNA recombination repair, whereas the Swi5-Swi2-Rhp51 interactions may function, together with chromodomain protein Swi6 (HP1 homolog), in mating-type switching.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14663140-10357855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14663140-10408447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14663140-10430583,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/14663140-9928492
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15770-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14663140-Amino Acid Sequence,
pubmed-meshheading:14663140-Animals,
pubmed-meshheading:14663140-Base Sequence,
pubmed-meshheading:14663140-Cloning, Molecular,
pubmed-meshheading:14663140-Crosses, Genetic,
pubmed-meshheading:14663140-DNA, Fungal,
pubmed-meshheading:14663140-DNA Primers,
pubmed-meshheading:14663140-DNA Repair,
pubmed-meshheading:14663140-Gamma Rays,
pubmed-meshheading:14663140-Genomic Library,
pubmed-meshheading:14663140-Humans,
pubmed-meshheading:14663140-Molecular Sequence Data,
pubmed-meshheading:14663140-Recombinant Proteins,
pubmed-meshheading:14663140-Recombination, Genetic,
pubmed-meshheading:14663140-Schizosaccharomyces,
pubmed-meshheading:14663140-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:14663140-Sequence Alignment,
pubmed-meshheading:14663140-Sequence Homology, Amino Acid,
pubmed-meshheading:14663140-Sequence Homology, Nucleic Acid,
pubmed-meshheading:14663140-Ultraviolet Rays
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pubmed:year |
2003
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pubmed:articleTitle |
Two different Swi5-containing protein complexes are involved in mating-type switching and recombination repair in fission yeast.
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pubmed:affiliation |
Graduate School of Integrated Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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