rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2004-10-15
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pubmed:abstractText |
In budding yeast most Rad51-dependent and -independent recombination depends on Rad52. In contrast, its homologue in fission yeast, Rad22, was assumed to play a less critical role possibly due to functional redundancy with another Rad52-like protein Rti1. We show here that this is not the case. Rad22 like Rad52 plays a central role in recombination being required for both Rhp51-dependent and -independent events. Having established this we proceed to investigate the involvement of the Mus81-Eme1 endonuclease in these pathways. Mus81 plays a relatively minor role in the Rhp51-dependent repair of DNA damage induced by ultraviolet light. In contrast Mus81 has a key role in the Rad22-dependent (Rhp51-independent) repair of damage induced by camptothecin, hydroxyurea and methyl-methanesulfonate. Furthermore, spontaneous intrachromosomal recombination that gives rise to deletion recombinants is impaired in a mus81 mutant. From these data we propose that a Rad22-Mus81-dependent (Rhp51-independent) pathway is an important mechanism for the repair of DNA damage in fission yeast. Consistent with this we show that in vitro Rad22 can promote strand invasion to form a D-loop that can be cleaved by Mus81.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15486206-10357855,
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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/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eme1protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Endonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/MUS81 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RHP51 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Rad22 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Rad51 Recombinase,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5570-81
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15486206-DNA, Fungal,
pubmed-meshheading:15486206-DNA Repair,
pubmed-meshheading:15486206-DNA-Binding Proteins,
pubmed-meshheading:15486206-Endonucleases,
pubmed-meshheading:15486206-Models, Genetic,
pubmed-meshheading:15486206-Mutation,
pubmed-meshheading:15486206-Nucleic Acid Conformation,
pubmed-meshheading:15486206-Rad51 Recombinase,
pubmed-meshheading:15486206-Recombination, Genetic,
pubmed-meshheading:15486206-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:15486206-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15486206-Schizosaccharomyces,
pubmed-meshheading:15486206-Schizosaccharomyces pombe Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
DNA repair by a Rad22-Mus81-dependent pathway that is independent of Rhp51.
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pubmed:affiliation |
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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