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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-1-1
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pubmed:abstractText |
We have previously reported about a new Saccharomyces cerevisiae mutation, hsm2-1, that results in increase of both spontaneous and UV-induced mutation frequencies but does not alter UV-sensitivity. Now HSM2 gene has been genetically and physically mapped and identified as a gene previously characterized as HMO1, a yeast homologue of human high mobility group genes HMG1/2. We found that hsm2 mutant is slightly deficient in plasmid-borne mismatch repair. We tested UV-induced mutagenesis in double mutants carrying hsm2-1 mutation and a mutation in a gene of principal damaged DNA repair pathways (rad2 and rev3) or in a mismatch repair gene (pms1 and recently characterized in our laboratory hsm3). The frequency of UV-induced mutations in hsm2 rev3 was not altered in comparison with single rev3 mutant. In contrast, the interaction of hsm2-1 with rad2 and pms1 was characterized by an increased frequency of UV-induced mutations in comparison with single rad2 and pms1 mutants. The UV-induced mutation frequency in double hsm2 hsm3 mutant was lower than in the single hsm2 and hsm3 mutants. The role of the HSM2 gene product in control of mutagenesis is discussed.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Fungal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
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/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HMO1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/HSM3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PMS1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/PMS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RAD2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/REV3 protein, S cerevisiae,
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 |
1568-7864
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
287-97
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12509247-Base Pair Mismatch,
pubmed-meshheading:12509247-Carrier Proteins,
pubmed-meshheading:12509247-Cell Survival,
pubmed-meshheading:12509247-DNA, Fungal,
pubmed-meshheading:12509247-DNA Damage,
pubmed-meshheading:12509247-DNA Primers,
pubmed-meshheading:12509247-DNA Repair,
pubmed-meshheading:12509247-DNA-Binding Proteins,
pubmed-meshheading:12509247-DNA-Directed DNA Polymerase,
pubmed-meshheading:12509247-Endodeoxyribonucleases,
pubmed-meshheading:12509247-Fungal Proteins,
pubmed-meshheading:12509247-Genes, Fungal,
pubmed-meshheading:12509247-High Mobility Group Proteins,
pubmed-meshheading:12509247-Molecular Chaperones,
pubmed-meshheading:12509247-Mutagenesis,
pubmed-meshheading:12509247-Mutation,
pubmed-meshheading:12509247-Neoplasm Proteins,
pubmed-meshheading:12509247-Polymerase Chain Reaction,
pubmed-meshheading:12509247-Saccharomyces cerevisiae,
pubmed-meshheading:12509247-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12509247-Ultraviolet Rays
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pubmed:year |
2002
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pubmed:articleTitle |
HSM2 (HMO1) gene participates in mutagenesis control in yeast Saccharomyces cerevisiae.
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pubmed:affiliation |
Laboratory of Eucaryote Genetics, Division of Molecular and Radiation Biophysics, Petersburg Nuclear Physics Institute, RAS, Leningrad distr., 188350, Gatchina, Orlova Roscha, Russia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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