Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2005-5-13
pubmed:abstractText
Transcriptional repression of the silent mating-type loci HMLalpha and HMRa in Saccharomyces cerevisiae is regulated by chromatin structure. Sas2p is a catalytic subunit of the SAS histone acetyltransferase (HAT) complex. Although many HATs seem to relieve chromosomal repression to facilitate transcriptional activation, sas mutant phenotypes include loss of SIR1-dependent silencing of HMLalpha. To gain insight into the mechanism of the SAS complex mediated silencing at HMLalpha, we investigated the expression and chromatin structure of the alpha2 gene in the HMLalpha locus. We found that deletion of SAS2 in combination with a null allele of SIR1 changed the chromatin structure of the precisely positioned nucleosome, which includes the mRNA start site of the alpha2 gene and derepressed alpha2 transcription. The Sas2p HAT domain was required for this silencing. Furthermore, chromatin immunoprecipitation analysis revealed that the SAS complex was associated with the HMLalpha locus, and ASF1 (which encodes chromatin assembly factor Asf1p), but not SIR1 and SIR2, was necessary for this localization. These data suggest that the HAT activity and ASF1-dependent localization of the SAS complex are required for SIR1-dependent HMLalpha silencing.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-10384305, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-10471697, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-10579938, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-10619427, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-10693811, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-10839822, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-11404324, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-11448965, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-11731479, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-11731480, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-11909520, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-11917007, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12093919, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12134062, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12379856, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12381660, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12410229, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12626510, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-12801725, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-14562106, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-15659401, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-2005823, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-2684414, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-8622770, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-8782818, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-9250679, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-9610415, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-9710623, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-9717241, http://linkedlifedata.com/resource/pubmed/commentcorrection/15891116-9740719
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ASF1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MATA2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SIR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SIR2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sas2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Silent Information Regulator..., http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 2, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins
pubmed:status
MEDLINE
pubmed:issn
1362-4962
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2742-50
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15891116-Acetyltransferases, pubmed-meshheading:15891116-Cell Cycle Proteins, pubmed-meshheading:15891116-Gene Deletion, pubmed-meshheading:15891116-Gene Expression Regulation, Fungal, pubmed-meshheading:15891116-Histone Acetyltransferases, pubmed-meshheading:15891116-Histone Deacetylases, pubmed-meshheading:15891116-Homeodomain Proteins, pubmed-meshheading:15891116-Molecular Chaperones, pubmed-meshheading:15891116-Nucleosomes, pubmed-meshheading:15891116-Promoter Regions, Genetic, pubmed-meshheading:15891116-Repressor Proteins, pubmed-meshheading:15891116-Saccharomyces cerevisiae, pubmed-meshheading:15891116-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15891116-Silent Information Regulator Proteins, Saccharomyces..., pubmed-meshheading:15891116-Sirtuin 2, pubmed-meshheading:15891116-Sirtuins
pubmed:year
2005
pubmed:articleTitle
Chromatin assembly factor Asf1p-dependent occupancy of the SAS histone acetyltransferase complex at the silent mating-type locus HMLalpha.
pubmed:affiliation
Laboratory of Environmental Biochemistry, Graduate School of Pharmaceutical Sciences, Osaka University 1-6 Yamada-Oka, Suita, Osaka 565-0871, Japan. osada@phs.osaka-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't