Source:http://linkedlifedata.com/resource/pubmed/id/10323239
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1999-5-24
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pubmed:abstractText |
The deduced protein product of the Bacillus subtilis gene yqfI, which is 255 residues long, shares homology (25% identity) with the Escherichia coli RecO protein. A null allele of yqfI, when present in an otherwise Rec+ B. subtilis strain, causes cells to become highly sensitive to DNA-damaging agents, and plasmid transformation (intramolecular recombination) is reduced by 25-fold while chromosomal transformation (intermolecular recombination) is only moderately affected (2.5-fold reduction). Therefore, the yqfI gene was renamed recO and its null allele is referred to as recO1. The recO1 mutation was introduced into recombination-deficient strains representative of the epistatic groups alpha (recF, recR and recL strains), beta (addA5 addB72), gamma (recH342) and epsilon (recU40). The recO mutation did not affect the sensitivity of recF, recR or recL cells to DNA-damaging agents, increased the sensitivity of recU and addAB cells and abolished the DNA repair capacity of recH cells. The recO mutation did not affect intermolecular recombination in recF, recL, recH or recU cells, but reduced (by about 9-fold) the incidence of intermolecular recombination in addAB cells. The recO mutation did not affect intramolecular recombination in the addAB, recU, recF or recL cells, but reduced it by about 75-fold in recH cells. The defects caused by the recO1 mutation can be partially suppressed by a common suppressor of the recF, recL and recR phenotypes. We therefore assigned recO to epistatic group alpha and predict that the RecO protein acts at the same stage of recombination as the RecF, RecL and RecR proteins, in a RecFLOR complex.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Methyl Methanesulfonate,
http://linkedlifedata.com/resource/pubmed/chemical/Mutagens,
http://linkedlifedata.com/resource/pubmed/chemical/RecO protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/RecR protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/RecR protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/recF protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/recF protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0026-8925
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
261
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
567-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10323239-Bacillus subtilis,
pubmed-meshheading:10323239-Bacterial Proteins,
pubmed-meshheading:10323239-DNA Repair,
pubmed-meshheading:10323239-DNA-Binding Proteins,
pubmed-meshheading:10323239-Escherichia coli,
pubmed-meshheading:10323239-Escherichia coli Proteins,
pubmed-meshheading:10323239-Genes, Bacterial,
pubmed-meshheading:10323239-Methyl Methanesulfonate,
pubmed-meshheading:10323239-Mutagens,
pubmed-meshheading:10323239-Mutation,
pubmed-meshheading:10323239-Phenotype,
pubmed-meshheading:10323239-Recombination, Genetic,
pubmed-meshheading:10323239-Species Specificity,
pubmed-meshheading:10323239-Suppression, Genetic
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pubmed:year |
1999
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pubmed:articleTitle |
Analysis of the Bacillus subtilis recO gene: RecO forms part of the RecFLOR function.
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pubmed:affiliation |
Department of Microbial Biotechnology, Centro Nacional de Biotecnología CSIC, Campus Universidad Autónoma de Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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