rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2001-11-9
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pubmed:abstractText |
Histone H3 lysine 9 methylation has been proposed to provide a major "switch" for the functional organization of chromosomal subdomains. Here, we show that the murine Suv39h histone methyltransferases (HMTases) govern H3-K9 methylation at pericentric heterochromatin and induce a specialized histone methylation pattern that differs from the broad H3-K9 methylation present at other chromosomal regions. Suv39h-deficient mice display severely impaired viability and chromosomal instabilities that are associated with an increased tumor risk and perturbed chromosome interactions during male meiosis. These in vivo data assign a crucial role for pericentric H3-K9 methylation in protecting genome stability, and define the Suv39h HMTases as important epigenetic regulators for mammalian development.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Nov
|
pubmed:issn |
0092-8674
|
pubmed:author |
pubmed-author:DoyleMM,
pubmed-author:JenuweinTT,
pubmed-author:KohlmaierAA,
pubmed-author:LachnerMM,
pubmed-author:MechtlerKK,
pubmed-author:O'CarrollDD,
pubmed-author:OpravilSS,
pubmed-author:PaganoGG,
pubmed-author:PetersA HAH,
pubmed-author:SauerSS,
pubmed-author:SchöferCC,
pubmed-author:ScherthanHH,
pubmed-author:SibiliaMM,
pubmed-author:WeipoltshammerKK
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pubmed:issnType |
Print
|
pubmed:day |
2
|
pubmed:volume |
107
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
323-37
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11701123-Aneuploidy,
pubmed-meshheading:11701123-Animals,
pubmed-meshheading:11701123-Chromosome Segregation,
pubmed-meshheading:11701123-Fibroblasts,
pubmed-meshheading:11701123-Gene Targeting,
pubmed-meshheading:11701123-Genome,
pubmed-meshheading:11701123-Germ Cells,
pubmed-meshheading:11701123-Heterochromatin,
pubmed-meshheading:11701123-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:11701123-Histones,
pubmed-meshheading:11701123-Hypogonadism,
pubmed-meshheading:11701123-Lymphoma, B-Cell,
pubmed-meshheading:11701123-Male,
pubmed-meshheading:11701123-Mammals,
pubmed-meshheading:11701123-Meiosis,
pubmed-meshheading:11701123-Methylation,
pubmed-meshheading:11701123-Methyltransferases,
pubmed-meshheading:11701123-Mice,
pubmed-meshheading:11701123-Mice, Knockout,
pubmed-meshheading:11701123-Mice, Mutant Strains,
pubmed-meshheading:11701123-Mutagenesis,
pubmed-meshheading:11701123-Protein Methyltransferases,
pubmed-meshheading:11701123-Repressor Proteins,
pubmed-meshheading:11701123-Sex Chromosome Aberrations,
pubmed-meshheading:11701123-Spermatocytes,
pubmed-meshheading:11701123-Spermatogenesis
|
pubmed:year |
2001
|
pubmed:articleTitle |
Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability.
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pubmed:affiliation |
Research Institute of Molecular Pathology (IMP), Vienna Biocenter, Dr. Bohrgasse 7, A-1030, Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|