pubmed-article:16618800 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16618800 | lifeskim:mentions | umls-concept:C1623167 | lld:lifeskim |
pubmed-article:16618800 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:16618800 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:16618800 | pubmed:dateCreated | 2006-5-2 | lld:pubmed |
pubmed-article:16618800 | pubmed:abstractText | Polycomb response elements (PREs) are specific cis-regulatory sequences needed for transcriptional repression of HOX and other target genes by Polycomb group (PcG) proteins. Among the many PcG proteins known in Drosophila, Pho is the only sequence-specific DNA-binding protein. To gain insight into the function of Pho, we purified Pho protein complexes from Drosophila embryos and found that Pho exists in two distinct protein assemblies: a Pho-dINO80 complex containing the Drosophila INO80 nucleosome-remodeling complex, and a Pho-repressive complex (PhoRC) containing the uncharacterized gene product dSfmbt. Analysis of PhoRC reveals that dSfmbt is a novel PcG protein that is essential for HOX gene repression in Drosophila. PhoRC is bound at HOX gene PREs in vivo, and this targeting strictly depends on Pho-binding sites. Characterization of dSfmbt protein shows that its MBT repeats have unique discriminatory binding activity for methylated lysine residues in histones H3 and H4; the MBT repeats bind mono- and di-methylated H3-K9 and H4-K20 but fail to interact with these residues if they are unmodified or tri-methylated. Our results establish PhoRC as a novel Drosophila PcG protein complex that combines DNA-targeting activity (Pho) with a unique modified histone-binding activity (dSfmbt). We propose that PRE-tethered PhoRC selectively interacts with methylated histones in the chromatin flanking PREs to maintain a Polycomb-repressed chromatin state. | lld:pubmed |
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pubmed-article:16618800 | pubmed:language | eng | lld:pubmed |
pubmed-article:16618800 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16618800 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16618800 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16618800 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16618800 | pubmed:month | May | lld:pubmed |
pubmed-article:16618800 | pubmed:issn | 0890-9369 | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:FischleWolfga... | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:SchelderMalgo... | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:WilmMatthiasM | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:KöcherThomasT | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:MüllerJürgJ | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:WildBrigitteB | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:FritschCornel... | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:KlymenkoTetya... | lld:pubmed |
pubmed-article:16618800 | pubmed:author | pubmed-author:PappBernadett... | lld:pubmed |
pubmed-article:16618800 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16618800 | pubmed:day | 1 | lld:pubmed |
pubmed-article:16618800 | pubmed:volume | 20 | lld:pubmed |
pubmed-article:16618800 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16618800 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16618800 | pubmed:pagination | 1110-22 | lld:pubmed |
pubmed-article:16618800 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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