Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-5-19
pubmed:databankReference
pubmed:abstractText
Intracellular energy balance is important for cell survival. In eukaryotic cells, the most energy-consuming process is ribosome biosynthesis, which adapts to changes in intracellular energy status. However, the mechanism that links energy status and ribosome biosynthesis is largely unknown. Here, we describe eNoSC, a protein complex that senses energy status and controls rRNA transcription. eNoSC contains Nucleomethylin, which binds histone H3 dimethylated Lys9 in the rDNA locus, in a complex with SIRT1 and SUV39H1. Both SIRT1 and SUV39H1 are required for energy-dependent transcriptional repression, suggesting that a change in the NAD(+)/NADH ratio induced by reduction of energy status could activate SIRT1, leading to deacetylation of histone H3 and dimethylation at Lys9 by SUV39H1, thus establishing silent chromatin in the rDNA locus. Furthermore, eNoSC promotes restoration of energy balance by limiting rRNA transcription, thus protecting cells from energy deprivation-dependent apoptosis. These findings provide key insight into the mechanisms of energy homeostasis in cells.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Ribosomal, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes, http://linkedlifedata.com/resource/pubmed/chemical/NAD, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SIRT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/SUV39H1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuin 1, http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins, http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1097-4172
pubmed:author
pubmed:issnType
Electronic
pubmed:day
16
pubmed:volume
133
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
627-39
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18485871-Cell Death, pubmed-meshheading:18485871-Cell Line, pubmed-meshheading:18485871-Cell Nucleolus, pubmed-meshheading:18485871-DNA, Ribosomal, pubmed-meshheading:18485871-Energy Metabolism, pubmed-meshheading:18485871-Gene Silencing, pubmed-meshheading:18485871-Glucose, pubmed-meshheading:18485871-Histone-Lysine N-Methyltransferase, pubmed-meshheading:18485871-Histones, pubmed-meshheading:18485871-Humans, pubmed-meshheading:18485871-Methyltransferases, pubmed-meshheading:18485871-Models, Molecular, pubmed-meshheading:18485871-Molecular Sequence Data, pubmed-meshheading:18485871-Multiprotein Complexes, pubmed-meshheading:18485871-NAD, pubmed-meshheading:18485871-Nuclear Proteins, pubmed-meshheading:18485871-Protein Methyltransferases, pubmed-meshheading:18485871-Protein Structure, Tertiary, pubmed-meshheading:18485871-Repressor Proteins, pubmed-meshheading:18485871-Sirtuin 1, pubmed-meshheading:18485871-Sirtuins, pubmed-meshheading:18485871-Transcription, Genetic
pubmed:year
2008
pubmed:articleTitle
Epigenetic control of rDNA loci in response to intracellular energy status.
pubmed:affiliation
Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8572, Japan.
pubmed:publicationType
Journal Article