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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0011155,
umls-concept:C0012940,
umls-concept:C0014834,
umls-concept:C0026882,
umls-concept:C0034767,
umls-concept:C0036667,
umls-concept:C0059946,
umls-concept:C0079866,
umls-concept:C0080194,
umls-concept:C0087111,
umls-concept:C0312418,
umls-concept:C0441889,
umls-concept:C1157894,
umls-concept:C1280500
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pubmed:issue |
1
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pubmed:dateCreated |
1983-7-29
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pubmed:abstractText |
Certain strains suppress the temperature-sensitivity caused by ssb-1, which encodes a mutant ssDNA binding protein (SSB). At 42 degrees C, such strains are extremely UV-sensitive, degrade their DNA extensively after UV irradiation, and are deficient in UV mutability and UV induction of recA protein synthesis. We transduced recC22, which eliminates Exonuclease V activity, and recAo281, which causes operator-constitutive synthesis of recA protein, into such an ssb-1 strain. Both double mutants degraded their DNA extensively at 42 degrees C after UV irradiation, and both were even more UV-sensitive than the ssb-1 single mutant. We conclude that one or more nucleases other than Exonuclease V degrades DNA in the ssb recC strain, and that recA protein, even if synthesized copiously, can function efficiently in recombinational DNA repair and in control of post-UV DNA degradation only if normal SSB is also present. Pretreatment with nalidixic acid at 30 degrees C restored normal UV mutability at 42 degrees C, but did not increase UV resistance, in an ssb-1 strain. Another ssb allele, ssb-113, which blocks SOS induction at 30 degrees C, increases spontaneous mutability more than tenfold. The ssb-113 allele was transduced into the SOS-constitutive recA730 strain SC30. This double mutant expressed the same elevated spontaneous and UV-induced mutability at 30 degrees C as the ssb+ recA730 strain, and was three times more UV-resistant than its ssb-113 recA+ parent. We conclude that ssb-1 at 42 degrees C and ssb-113 at 30 degrees C block UV-induced activation of recA protease, but that neither allele interferes with subsequent steps in SOS-mediated mutagenesis.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonuclease V,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Nalidixic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Rec A Recombinases,
http://linkedlifedata.com/resource/pubmed/chemical/exodeoxyribonuclease V, E coli
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pubmed:status |
MEDLINE
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pubmed:issn |
0026-8925
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
190
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
92-100
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6343804-Bacterial Proteins,
pubmed-meshheading:6343804-Carrier Proteins,
pubmed-meshheading:6343804-DNA, Bacterial,
pubmed-meshheading:6343804-DNA Repair,
pubmed-meshheading:6343804-DNA Replication,
pubmed-meshheading:6343804-Escherichia coli,
pubmed-meshheading:6343804-Escherichia coli Proteins,
pubmed-meshheading:6343804-Exodeoxyribonuclease V,
pubmed-meshheading:6343804-Exodeoxyribonucleases,
pubmed-meshheading:6343804-Mutation,
pubmed-meshheading:6343804-Nalidixic Acid,
pubmed-meshheading:6343804-Rec A Recombinases,
pubmed-meshheading:6343804-Ultraviolet Rays
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pubmed:year |
1983
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pubmed:articleTitle |
DNA degradation, UV sensitivity and SOS-mediated mutagenesis in strains of Escherichia coli deficient in single-strand DNA binding protein: effects of mutations and treatments that alter levels of Exonuclease V or recA protein.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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