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Vermeulen, Michiel; Eberl, H. Christian; Matarese, Filomena; Marks, Hendrik; Denissov, Sergei; Butter, Falk; Lee, Kenneth K.; Olsen, Jesper V.; Hyman, Anthony A.; Stunnenberg, Henk G.; Mann, Matthias
Cell, 09/2010, Letnik: 142, Številka: 6Journal Article
Trimethyl-lysine (me3) modifications on histones are the most stable epigenetic marks and they control chromatin-mediated regulation of gene expression. Here, we determine proteins that bind these marks by high-accuracy, quantitative mass spectrometry. These chromatin “readers” are assigned to complexes by interaction proteomics of full-length BAC-GFP-tagged proteins. ChIP-Seq profiling identifies their genomic binding sites, revealing functional properties. Among the main findings, the human SAGA complex binds to H3K4me3 via a double Tudor-domain in the C terminus of Sgf29, and the PWWP domain is identified as a putative H3K36me3 binding motif. The ORC complex, including LRWD1, binds to the three most prominent transcriptional repressive lysine methylation sites. Our data reveal a highly adapted interplay between chromatin marks and their associated protein complexes. Reading specific trimethyl-lysine sites by specialized complexes appears to be a widespread mechanism to mediate gene expression. Display omitted ► MS-based proteomics screen identifies novel histone lysine trimethylation readers ► Readers are assembled into complexes and their genome-wide occupancy is determined ► Sgf29 links the SAGA complex to H3K4me3 via a double tudor domain ► Trimethyl reader complexes determine the biological function of their epigenetic mark
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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