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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1996-6-21
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pubmed:abstractText |
Cell division in haploid yeast gives rise to a "mother" cell capable of mating-type switching and a "daughter" cell that is not. Switching is initiated by the HO endonuclease, whose gene is only transcribed in cells that have previously given birth to a bud (mother cells). HO expression depends on a minimyosin, She1p/Myo4p, which accumulates preferentially in growing buds. We describe a gene, ASH1, that is necessary to repress HO in daughters. ASH1 encodes a zinc finger protein whose preferential accumulation in daughter cell nuclei at the end of anaphase depends on She1p/Myo4p. The greater abundance of Ash1p in daughter cells is responsible for restricting HO expression to mother cells.
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pubmed:commentsCorrections |
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, Type II...,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HO protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Myo4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type V,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SCEI protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
699-709
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8625408-Amino Acid Sequence,
pubmed-meshheading:8625408-Anaphase,
pubmed-meshheading:8625408-Base Sequence,
pubmed-meshheading:8625408-Cell Nucleus,
pubmed-meshheading:8625408-Cloning, Molecular,
pubmed-meshheading:8625408-Crosses, Genetic,
pubmed-meshheading:8625408-DNA-Binding Proteins,
pubmed-meshheading:8625408-Deoxyribonucleases, Type II Site-Specific,
pubmed-meshheading:8625408-Epitopes,
pubmed-meshheading:8625408-Fungal Proteins,
pubmed-meshheading:8625408-Gene Expression,
pubmed-meshheading:8625408-Genes, Fungal,
pubmed-meshheading:8625408-Genes, Mating Type, Fungal,
pubmed-meshheading:8625408-Molecular Sequence Data,
pubmed-meshheading:8625408-Mutagenesis,
pubmed-meshheading:8625408-Myosin Heavy Chains,
pubmed-meshheading:8625408-Myosin Type V,
pubmed-meshheading:8625408-Myosins,
pubmed-meshheading:8625408-Open Reading Frames,
pubmed-meshheading:8625408-Recombinant Proteins,
pubmed-meshheading:8625408-Repressor Proteins,
pubmed-meshheading:8625408-Saccharomyces cerevisiae,
pubmed-meshheading:8625408-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8625408-Sequence Homology, Amino Acid,
pubmed-meshheading:8625408-Species Specificity,
pubmed-meshheading:8625408-Transcription, Genetic,
pubmed-meshheading:8625408-Transcription Factors,
pubmed-meshheading:8625408-Zinc Fingers
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pubmed:year |
1996
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pubmed:articleTitle |
Asymmetric accumulation of Ash1p in postanaphase nuclei depends on a myosin and restricts yeast mating-type switching to mother cells.
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pubmed:affiliation |
Research Institute of Molecular Pathology, Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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