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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2009-4-13
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pubmed:abstractText |
The deletion of the gene encoding the high mobility group protein Hmo1 suppresses the growth retardation of the DNA pol delta mutation, pol3-14, at the restrictive temperature. pol3-14 mutant cells undergo cell cycle arrest, and hmo1Delta alleviates the arrest permitting continual division of the double mutant. Bypass of cell cycle control occurs with an increased rate of mutation. Both pol3-14 and hmo1Delta are mutators and their combination provokes a synergistic rate of CAN1 mutations. RAD18 controls branches of DNA repair pathways and its deletion also suppresses pol3 mutations. Comparing hmo1Delta and rad18Delta suppression of pol3-14 shows that while both require the presence of RAD52-mediated repair, their suppression is independent in that both can suppress in the presence of the other. We conclude that hmo1Delta suppression of pol3-14 occurs by a mechanism whereby normal controls on DNA integrity are breached and lesions flow into RAD52-mediated repair and error-prone pathways.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Polymerase III,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HMO1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAD18 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD52 protein, S cerevisiae,
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:month |
Apr
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pubmed:issn |
1432-0983
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
127-38
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19184026-Adenosine Triphosphatases,
pubmed-meshheading:19184026-DNA Helicases,
pubmed-meshheading:19184026-DNA Polymerase III,
pubmed-meshheading:19184026-DNA Repair,
pubmed-meshheading:19184026-DNA-Binding Proteins,
pubmed-meshheading:19184026-Gene Deletion,
pubmed-meshheading:19184026-High Mobility Group Proteins,
pubmed-meshheading:19184026-Mutation,
pubmed-meshheading:19184026-Rad52 DNA Repair and Recombination Protein,
pubmed-meshheading:19184026-Saccharomyces cerevisiae,
pubmed-meshheading:19184026-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:19184026-Temperature,
pubmed-meshheading:19184026-Trinucleotide Repeats
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pubmed:year |
2009
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pubmed:articleTitle |
Suppression of a DNA polymerase delta mutation by the absence of the high mobility group protein Hmo1 in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, 55455, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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