Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-2-15
pubmed:abstractText
In the yeast Saccharomyces cerevisiae, Tup1, in association with Cyc8 (Ssn6), functions as a general transcriptional corepressor. This repression is mediated by recruitment of the Tup1-Cyc8 complex to target promoters through sequence-specific DNA-binding proteins such as Sko1, which mediates the HOG pathway-dependent regulation. We identified tup1 and cyc8 mutant alleles as the suppressor of osmo-sensitivity of the hog1Delta strain. In these mutants, although the expression of the genes under the control of DNA-binding proteins other than Sko1 was apparently normal, the Sko1-regulated genes GRE2 and AHP1 were derepressed under non-stress conditions, suggesting that the Tup1 and Cyc8 mutant proteins were specifically defective in the repression of the Sko1-dependent genes. Chromatin immunoprecipitation analyses of the GRE2 promoter in the mutants demonstrated that the Sko1-Tup1-Cyc8 complex was localized to the promoter, together with Gcn5/SAGA, suggesting that the erroneous recruitment of SAGA to the promoter led to the derepression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription..., http://linkedlifedata.com/resource/pubmed/chemical/CYC8 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GCN5 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/GRE2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/HOG1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SKO1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TUP1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
28
pubmed:volume
368
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18201562-Alleles, pubmed-meshheading:18201562-Basic-Leucine Zipper Transcription Factors, pubmed-meshheading:18201562-Calcium, pubmed-meshheading:18201562-DNA-Binding Proteins, pubmed-meshheading:18201562-Gene Expression Regulation, Fungal, pubmed-meshheading:18201562-Histone Acetyltransferases, pubmed-meshheading:18201562-Mitogen-Activated Protein Kinases, pubmed-meshheading:18201562-Mutation, pubmed-meshheading:18201562-Nuclear Proteins, pubmed-meshheading:18201562-Osmotic Pressure, pubmed-meshheading:18201562-Oxidoreductases, pubmed-meshheading:18201562-Promoter Regions, Genetic, pubmed-meshheading:18201562-Protein Binding, pubmed-meshheading:18201562-Repressor Proteins, pubmed-meshheading:18201562-Saccharomyces cerevisiae, pubmed-meshheading:18201562-Saccharomyces cerevisiae Proteins, pubmed-meshheading:18201562-Sensitivity and Specificity
pubmed:year
2008
pubmed:articleTitle
Identification of Tup1 and Cyc8 mutations defective in the responses to osmotic stress.
pubmed:affiliation
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8530, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't