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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2002-11-27
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pubmed:abstractText |
The DNA synthesis associated with recombinational repair of chromosomal double-strand breaks (DSBs) has a lower fidelity than normal replicative DNA synthesis. Here, we use an inverted-repeat substrate to monitor the fidelity of repair of a site-specific DSB. DSB induction made by the HO endonuclease stimulates recombination >5000-fold and is associated with a >1000-fold increase in mutagenesis of an adjacent gene. We demonstrate that most break-repair-induced mutations (BRIMs) are point mutations and have a higher proportion of frameshifts than do spontaneous mutations of the same substrate. Although the REV3 translesion DNA polymerase is not required for recombination, it introduces approximately 75% of the BRIMs and approximately 90% of the base substitution mutations. Recombinational repair of the DSB is strongly dependent upon genes of the RAD52 epistasis group; however, the residual recombinants present in rad57 mutants are associated with a 5- to 20-fold increase in BRIMs. The spectrum of mutations in rad57 mutants is similar to that seen in the wild-type strain and is similarly affected by REV3. We also find that REV3 is required for the repair of MMS-induced lesions when recombinational repair is compromised. Our data suggest that Rad55p/Rad57p help limit the generation of substrates that require pol zeta during recombination.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12454056-10082560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12454056-10220423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12454056-10357855,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/12454056-9881976
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pubmed:language |
eng
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAD51 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD52 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD57 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/REV3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Rad51 Recombinase,
http://linkedlifedata.com/resource/pubmed/chemical/Rad52 DNA Repair and Recombination...,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:author |
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1063-77
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pubmed:dateRevised |
2009-11-19
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pubmed:articleTitle |
The roles of REV3 and RAD57 in double-strand-break-repair-induced mutagenesis of Saccharomyces cerevisiae.
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pubmed:affiliation |
Gene Regulation and Chromosome Biology Laboratory, National Cancer Institute-Frederick Cancer Research and Development Center, Frederick, Maryland 21702, USA.
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