Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2008-12-8
pubmed:abstractText
The extensively studied yeast GAL1-10 gene cluster is tightly regulated by environmental sugar availability. Unexpectedly, under repressive conditions the 3' region of the GAL10 coding sequence is trimethylated by Set1 on histone H3 K4, normally characteristic of 5' regions of actively transcribed genes. This reflects transcription of a long noncoding RNA (GAL10-ncRNA) that is reciprocal to GAL1 and GAL10 mRNAs and driven by the DNA-binding protein Reb1. Point mutations in predicted Reb1-binding sites abolished Reb1 binding and ncRNA synthesis. The GAL10-ncRNA is transcribed approximately once every 50 min and targeted for degradation by the TRAMP and exosome complexes, resulting in low steady-state levels (approximately one molecule per 14 cells). GAL10-ncRNA transcription recruits the methyltransferase Set2 and histone deacetylation activities in cis, leading to stable changes in chromatin structure. These chromatin modifications act principally through the Rpd3S complex to aid glucose repression of GAL1-10 at physiologically relevant sugar concentrations.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eaf3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/REB1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Untranslated, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1097-4164
pubmed:author
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
685-95
pubmed:meshHeading
pubmed-meshheading:19061643-Acetyltransferases, pubmed-meshheading:19061643-Chromatin, pubmed-meshheading:19061643-DNA-Binding Proteins, pubmed-meshheading:19061643-Gene Expression Regulation, Fungal, pubmed-meshheading:19061643-Genes, Fungal, pubmed-meshheading:19061643-Glucose, pubmed-meshheading:19061643-Histones, pubmed-meshheading:19061643-Lysine, pubmed-meshheading:19061643-Methylation, pubmed-meshheading:19061643-Models, Biological, pubmed-meshheading:19061643-Multigene Family, pubmed-meshheading:19061643-Protein Processing, Post-Translational, pubmed-meshheading:19061643-RNA, Messenger, pubmed-meshheading:19061643-RNA, Untranslated, pubmed-meshheading:19061643-Repressor Proteins, pubmed-meshheading:19061643-Saccharomyces cerevisiae, pubmed-meshheading:19061643-Saccharomyces cerevisiae Proteins, pubmed-meshheading:19061643-Transcription, Genetic, pubmed-meshheading:19061643-Transcription Factors
pubmed:year
2008
pubmed:articleTitle
A ncRNA modulates histone modification and mRNA induction in the yeast GAL gene cluster.
pubmed:affiliation
Wellcome Trust Centre for Cell Biology, Institute for Cell Biology, University of Edinburgh, Edinburgh EH9 3JR, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural