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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2003-4-21
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pubmed:abstractText |
Imprinted genes in mammals are often located in clusters whose imprinting is subject to long range regulation by cis-acting sequences known as imprinting centers (ICs). The mechanisms by which these ICs exert their effects is unknown. The Prader-Willi syndrome IC (PWS-IC) on human chromosome 15 and mouse chromosome 7 regulates imprinted gene expression bidirectionally within an approximately 2-megabase region and shows CpG methylation and histone H3 Lys-9 methylation in somatic cells specific for the maternal chromosome. Here we show that histone H3 Lys-9 methylation of the PWS-IC is reduced in mouse embryonic stem (ES) cells lacking the G9a histone H3 Lys-9/Lys-27 methyltransferase and that maintenance of CpG methylation of the PWS-IC in mouse ES cells requires the function of G9a. We show by RNA fluorescence in situ hybridization (FISH) that expression of Snrpn, an imprinted gene regulated by the PWS-IC, is biallelic in G9a -/- ES cells, indicating loss of imprinting. By contrast, Dnmt1 -/- ES cells lack CpG methylation of the PWS-IC but have normal levels of H3 Lys-9 methylation of the PWS-IC and show normal monoallelic Snrpn expression. Our results demonstrate a role for histone methylation in the maintenance of parent-specific CpG methylation of imprinting regulatory regions and suggest a possible role of histone methylation in establishment of these CpG methylation patterns.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Dinucleoside Phosphates,
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/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/SNRPN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/cytidylyl-3'-5'-guanosine,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/snRNP Core Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14996-5000
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12586828-Animals,
pubmed-meshheading:12586828-Autoantigens,
pubmed-meshheading:12586828-Cell Line,
pubmed-meshheading:12586828-DNA Methylation,
pubmed-meshheading:12586828-Dinucleoside Phosphates,
pubmed-meshheading:12586828-Embryo, Mammalian,
pubmed-meshheading:12586828-Genomic Imprinting,
pubmed-meshheading:12586828-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:12586828-Histones,
pubmed-meshheading:12586828-In Situ Hybridization, Fluorescence,
pubmed-meshheading:12586828-Methyltransferases,
pubmed-meshheading:12586828-Mice,
pubmed-meshheading:12586828-Prader-Willi Syndrome,
pubmed-meshheading:12586828-Protein Methyltransferases,
pubmed-meshheading:12586828-Repressor Proteins,
pubmed-meshheading:12586828-Ribonucleoproteins, Small Nuclear,
pubmed-meshheading:12586828-Stem Cells,
pubmed-meshheading:12586828-Transgenes,
pubmed-meshheading:12586828-snRNP Core Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Role of histone methyltransferase G9a in CpG methylation of the Prader-Willi syndrome imprinting center.
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pubmed:affiliation |
Departments of Biochemistry and Molecular Genetics and Pediatrics, University of Virginia, Charlottesville, Virginia 22908-0733, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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