| pubmed-article:14663140 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14663140 | lifeskim:mentions | umls-concept:C0178453 | lld:lifeskim |
| pubmed-article:14663140 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
| pubmed-article:14663140 | lifeskim:mentions | umls-concept:C1158512 | lld:lifeskim |
| pubmed-article:14663140 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:14663140 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:14663140 | pubmed:dateCreated | 2003-12-24 | lld:pubmed |
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| pubmed-article:14663140 | 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. | lld:pubmed |
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| pubmed-article:14663140 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14663140 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14663140 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14663140 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14663140 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14663140 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:14663140 | pubmed:author | pubmed-author:IkeguchiMitsu... | lld:pubmed |
| pubmed-article:14663140 | pubmed:author | pubmed-author:IwasakiHirosh... | lld:pubmed |
| pubmed-article:14663140 | pubmed:author | pubmed-author:ShinagawaHide... | lld:pubmed |
| pubmed-article:14663140 | pubmed:author | pubmed-author:DziadkowiecDo... | lld:pubmed |
| pubmed-article:14663140 | pubmed:author | pubmed-author:AkamatsuYufuk... | lld:pubmed |
| pubmed-article:14663140 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14663140 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:14663140 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:14663140 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14663140 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14663140 | pubmed:pagination | 15770-5 | lld:pubmed |
| pubmed-article:14663140 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:14663140 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14663140 | pubmed:articleTitle | Two different Swi5-containing protein complexes are involved in mating-type switching and recombination repair in fission yeast. | lld:pubmed |
| pubmed-article:14663140 | pubmed:affiliation | Graduate School of Integrated Science, Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan. | lld:pubmed |
| pubmed-article:14663140 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14663140 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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