| pubmed-article:15550569 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15550569 | lifeskim:mentions | umls-concept:C0920533 | lld:lifeskim |
| pubmed-article:15550569 | lifeskim:mentions | umls-concept:C1156205 | lld:lifeskim |
| pubmed-article:15550569 | lifeskim:mentions | umls-concept:C1705810 | lld:lifeskim |
| pubmed-article:15550569 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:15550569 | pubmed:dateCreated | 2004-11-19 | lld:pubmed |
| pubmed-article:15550569 | pubmed:abstractText | Site-specific modification of nucleosomal histones plays a central role in the formation of transcriptionally active and inactive chromatin structures. These modifications may serve as specific recognition motifs for chromatin proteins, which act as a signal for the adoption of the appropriate regulatory responses. Here, we show that the orphan nuclear receptor SHP (small heterodimer partner), a coregulator that inhibits the activity of several nuclear receptors, can associate with unmodified and lysine 9-methylated histone-3, but not with the acetylated protein. The naturally occurring SHP mutant (R213C), which exhibits decreased transrepression potential, interacts less avidly with K9-methylated histone 3. We demonstrate that SHP can functionally interact with histone deacetylase-1 and the G9a methyltransferase and that it is localized exclusively in nuclease-sensitive euchromatin. The results point to the involvement of a multistep mechanism in SHP-dependent transcriptional repression, which includes histone deacetylation, followed by H3-K9 methylation and stable association of SHP itself with chromatin. | lld:pubmed |
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| pubmed-article:15550569 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15550569 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15550569 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15550569 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15550569 | pubmed:issn | 1362-4962 | lld:pubmed |
| pubmed-article:15550569 | pubmed:author | pubmed-author:TalianidisIan... | lld:pubmed |
| pubmed-article:15550569 | pubmed:author | pubmed-author:BouliasKonsta... | lld:pubmed |
| pubmed-article:15550569 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15550569 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:15550569 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15550569 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15550569 | pubmed:pagination | 6096-103 | lld:pubmed |
| pubmed-article:15550569 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15550569 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15550569 | pubmed:articleTitle | Functional role of G9a-induced histone methylation in small heterodimer partner-mediated transcriptional repression. | lld:pubmed |
| pubmed-article:15550569 | pubmed:affiliation | Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas, PO Box 1527, Vassilika Vouton, 711 10 Herakleion, Crete, Greece. | lld:pubmed |
| pubmed-article:15550569 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15550569 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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