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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1992-9-4
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pubmed:abstractText |
It has been previously shown both in vivo and in vitro that DNA synthesis past an oxidatively damaged form of guanine, 7,8-dihydro-8-oxoguanine (8-oxoG), can result in the misincorporation of adenine (A) opposite the 8-oxodG. In this study we show that MutY glycosylase is active on a site-specific, oxidatively damaged A/8-oxoG mispair and that it removes the undamaged adenine from this mispair. Strains that lack active MutY protein have elevated rates of G.C----T.A transversions. We find that the mutator phenotype of a mutY strain can be fully complemented by overexpressing MutM protein (Fpg protein) from a plasmid clone. The MutM protein removes 8-oxoG lesions from DNA. In addition, we have isolated a strain with a chromosomal mutation that suppresses the mutY phenotype and found that this suppressor also overexpresses MutM. Finally, a mutY mutM double mutant has a 25- to 75-fold higher mutation rate than either mutator alone. The data strongly suggest that MutY is part of an intricate repair system directed against 8-oxoG lesions in nucleic acids and that the primary function of MutY in vivo is the removal of adenines that are misincorporated opposite 8-oxoG lesions during DNA synthesis.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-1309939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-1649454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-1710617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-1992344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2029751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2052015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2052552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2223758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2352934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2429316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2501784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2682664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-2690930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-3053667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-3128795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1495996-5328724
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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 |
Aug
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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 |
1
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pubmed:volume |
89
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pubmed:geneSymbol |
mutM,
mutY
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7022-5
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1495996-Bacterial Proteins,
pubmed-meshheading:1495996-Base Composition,
pubmed-meshheading:1495996-Base Sequence,
pubmed-meshheading:1495996-DNA Damage,
pubmed-meshheading:1495996-DNA Glycosylases,
pubmed-meshheading:1495996-DNA Repair,
pubmed-meshheading:1495996-DNA Replication,
pubmed-meshheading:1495996-DNA-Formamidopyrimidine Glycosylase,
pubmed-meshheading:1495996-Escherichia coli,
pubmed-meshheading:1495996-Escherichia coli Proteins,
pubmed-meshheading:1495996-Genes, Bacterial,
pubmed-meshheading:1495996-Genetic Complementation Test,
pubmed-meshheading:1495996-Guanine,
pubmed-meshheading:1495996-Models, Genetic,
pubmed-meshheading:1495996-Molecular Sequence Data,
pubmed-meshheading:1495996-Mutation,
pubmed-meshheading:1495996-N-Glycosyl Hydrolases,
pubmed-meshheading:1495996-Oligodeoxyribonucleotides,
pubmed-meshheading:1495996-Plasmids
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pubmed:year |
1992
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pubmed:articleTitle |
Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA.
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pubmed:affiliation |
Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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