Source:http://linkedlifedata.com/resource/pubmed/id/16702210
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
29
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| pubmed:dateCreated |
2006-7-17
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| pubmed:abstractText |
G9a is a SET-domain mammalian histone methyltransferase responsible for mono- and dimethylation of lysine 9 in histone H3 (H3K9) at euchromatic regions. Recently we reported that G9a forms a stoichiometric heteromeric complex with another SET-domain-containing molecule, GLP/Eu-HMTase1. Although G9a and GLP can independently methylate H3K9 in vitro, G9a/GLP heteromeric formation seems to be essential for their function as a euchromatic H3K9 methyltransferase in vivo. To further elucidate how G9a/GLP-mediated histone methylation and transcriptional regulation are controlled, we purified and characterized G9a complexes from mouse embryonic stem cells. We identified a novel G9a/GLP-associating zinc finger molecule named Wiz that can interact with G9a and GLP independently but is more stable in the G9a/GLP heteromeric complexes. Interestingly, Wiz small inhibitory RNA knocks down not only Wiz but also G9a. GLP deficiency also decreases G9a levels, suggesting that the Wiz/G9a/GLP tri-complex may protect G9a from degradation and that Wiz plays a major role in G9a/GLP heterodimer formation. Furthermore, amino acid sequence analysis of Wiz predicted two potential CtBP binding sites, and indeed CtBP binding to Wiz and association of CtBP with the Wiz/G9a/GLP complex was observed. These data indicate that Wiz not only contributes to the stability of G9a but also links the G9a/GLP heteromeric complex to the CtBP co-repressor machinery.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/GLP protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Kruppel-Like Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Wiz protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
21
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| pubmed:volume |
281
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
20120-8
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:16702210-Amino Acid Sequence,
pubmed-meshheading:16702210-Animals,
pubmed-meshheading:16702210-Base Sequence,
pubmed-meshheading:16702210-Cell Line,
pubmed-meshheading:16702210-Cells, Cultured,
pubmed-meshheading:16702210-DNA Primers,
pubmed-meshheading:16702210-Dimerization,
pubmed-meshheading:16702210-Gene Silencing,
pubmed-meshheading:16702210-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:16702210-Kruppel-Like Transcription Factors,
pubmed-meshheading:16702210-Mice,
pubmed-meshheading:16702210-Molecular Sequence Data,
pubmed-meshheading:16702210-Nerve Tissue Proteins,
pubmed-meshheading:16702210-Protein Methyltransferases,
pubmed-meshheading:16702210-Repressor Proteins,
pubmed-meshheading:16702210-Stem Cells,
pubmed-meshheading:16702210-Transcription, Genetic,
pubmed-meshheading:16702210-Transcription Factors
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| pubmed:year |
2006
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| pubmed:articleTitle |
Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP.
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| pubmed:affiliation |
Experimental Research Center for Infectious Diseases, Institute for Virus Research, Kyoto University, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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