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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5616
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pubmed:dateCreated |
2003-4-4
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pubmed:abstractText |
The Polycomb group (PcG) protein Eed is implicated in regulation of imprinted X-chromosome inactivation in extraembryonic cells but not of random X inactivation in embryonic cells. The Drosophila homolog of the Eed-Ezh2 PcG protein complex achieves gene silencing through methylation of histone H3 on lysine 27 (H3-K27), which suggests a role for H3-K27 methylation in imprinted X inactivation. Here we demonstrate that transient recruitment of the Eed-Ezh2 complex to the inactive X chromosome (Xi) occurs during initiation of X inactivation in both extraembryonic and embryonic cells and is accompanied by H3-K27 methylation. Recruitment of the complex and methylation on the Xi depend on Xist RNA but are independent of its silencing function. Together, our results suggest a role for Eed-Ezh2-mediated H3-K27 methylation during initiation of both imprinted and random X inactivation and demonstrate that H3-K27 methylation is not sufficient for silencing of the Xi.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
4
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pubmed:volume |
300
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-5
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:12649488-Animals,
pubmed-meshheading:12649488-Blastocyst,
pubmed-meshheading:12649488-Cell Differentiation,
pubmed-meshheading:12649488-Cell Nucleus,
pubmed-meshheading:12649488-Cells, Cultured,
pubmed-meshheading:12649488-Dosage Compensation, Genetic,
pubmed-meshheading:12649488-Female,
pubmed-meshheading:12649488-Fluorescent Antibody Technique,
pubmed-meshheading:12649488-Genomic Imprinting,
pubmed-meshheading:12649488-HeLa Cells,
pubmed-meshheading:12649488-Histones,
pubmed-meshheading:12649488-Humans,
pubmed-meshheading:12649488-In Situ Hybridization, Fluorescence,
pubmed-meshheading:12649488-Lysine,
pubmed-meshheading:12649488-Male,
pubmed-meshheading:12649488-Methylation,
pubmed-meshheading:12649488-Mice,
pubmed-meshheading:12649488-Mutation,
pubmed-meshheading:12649488-RNA, Untranslated,
pubmed-meshheading:12649488-Repressor Proteins,
pubmed-meshheading:12649488-Stem Cells,
pubmed-meshheading:12649488-Transgenes,
pubmed-meshheading:12649488-Trophoblasts,
pubmed-meshheading:12649488-X Chromosome
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pubmed:year |
2003
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pubmed:articleTitle |
Role of histone H3 lysine 27 methylation in X inactivation.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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