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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1994-3-25
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pubmed:databankReference |
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pubmed:abstractText |
The pattern of mating-type switching in cell pedigrees of the fission yeast Schizosaccharomyces pombe is dictated by the inheritance of specific DNA chains at the mating-type locus (mat1). The recombination event essential for switching is initiated by a site-specific double-strand break at mat1. The switch-activating protein, Sap1, binds in vitro to a mat1 cis-acting site that was shown earlier to be essential for efficient mating-type switching. We isolated the sap1 gene by using oligonucleotides corresponding to the amino acid sequence of purified Sap1 protein. The sequence of that gene predicted a 30-kDa protein with no significant homology to other canonical DNA-binding protein motifs. To facilitate its biochemical characterization, Sap1 was expressed in Escherichia coli. The protein expressed in bacteria displayed the same DNA-binding specificities as the protein purified from S. pombe. Interestingly, analysis of a sap1 null mutation showed that the gene is essential for growth even in a strain in which mating-type switching is prohibited because of a defect in generation of the double-strand break. Thus, the sap1 gene product implicated in mating-type switching is shown to be essential for cell viability.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-1195397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-17248996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-1915277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2005825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2016051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2328720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2421409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2645138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2659437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2714252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2876518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2900761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-2996882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-3162770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-3461465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-354496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-3561486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-3742597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-3909145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-4040853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-6236744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-6310324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-6322425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-6325178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-6348555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-6587363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-7042099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-8423854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-8431959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8114737-859590
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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 |
Mar
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:geneSymbol |
RAD50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2058-65
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:8114737-Amino Acid Sequence,
pubmed-meshheading:8114737-Base Sequence,
pubmed-meshheading:8114737-Cloning, Molecular,
pubmed-meshheading:8114737-DNA-Binding Proteins,
pubmed-meshheading:8114737-Fungal Proteins,
pubmed-meshheading:8114737-Gene Expression Regulation, Fungal,
pubmed-meshheading:8114737-Genes, Fungal,
pubmed-meshheading:8114737-Genes, Mating Type, Fungal,
pubmed-meshheading:8114737-Molecular Sequence Data,
pubmed-meshheading:8114737-Mutagenesis, Insertional,
pubmed-meshheading:8114737-Oligodeoxyribonucleotides,
pubmed-meshheading:8114737-Protein Structure, Secondary,
pubmed-meshheading:8114737-RNA, Messenger,
pubmed-meshheading:8114737-Schizosaccharomyces,
pubmed-meshheading:8114737-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:8114737-Sequence Alignment,
pubmed-meshheading:8114737-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
Sap1, a protein that binds to sequences required for mating-type switching, is essential for viability in Schizosaccharomyces pombe.
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pubmed:affiliation |
Laboratory of Eukaryotic Gene Expression, NCI-Frederick Cancer Research and Development Center, Maryland 21702-1201.
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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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