Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association
about
Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27Epigenetic virtues of chromodomainsHP1 recruits activity-dependent neuroprotective protein to H3K9me3 marked pericentromeric heterochromatin for silencing of major satellite repeatsH3K9me2/3 binding of the MBT domain protein LIN-61 is essential for Caenorhabditis elegans vulva developmentThe testis-enriched histone demethylase, KDM4D, regulates methylation of histone H3 lysine 9 during spermatogenesis in the mouse but is dispensable for fertilityHeterochromatin-associated interactions of Drosophila HP1a with dADD1, HIPP1, and repetitive RNAs.Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription.Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly.Cdyl, a new partner of the inactive X chromosome and potential reader of H3K27me3 and H3K9me2.Reader interactome of epigenetic histone marks in birds.The making of a Barr body: the mosaic of factors that eXIST on the mammalian inactive X chromosome.Chromodomain protein CDYL is required for transmission/restoration of repressive histone marks.Identification of protein complexes that bind to histone H3 combinatorial modifications using super-SILAC and weighted correlation network analysis.Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patterns.The proteomic investigation of chromatin functional domains reveals novel synergisms among distinct heterochromatin components.Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions.Short-Form CDYLb but not long-form CDYLa functions cooperatively with histone methyltransferase G9a in hepatocellular carcinomas.Quantitative and Structural Assessment of Histone Methyllysine Analogue Engagement by Cognate Binding Proteins Reveals Affinity Decrements Relative to Those of Native Counterparts.CDYL1 fosters double-strand break-induced transcription silencing and promotes homology-directed repair.Deciphering and engineering chromodomain-methyllysine peptide recognition
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P2860
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 05 October 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association
@en
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association.
@nl
type
label
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association
@en
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association.
@nl
prefLabel
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association
@en
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association.
@nl
P2093
P2860
P356
P1476
Multimerization and H3K9me3 binding are required for CDYL1b heterochromatin association
@en
P2093
Henning Urlaub
Henriette Franz
Kerstin Mosch
Szabolcs Soeroes
Wolfgang Fischle
P2860
P304
35049-35059
P356
10.1074/JBC.M109.052332
P407
P577
2009-10-05T00:00:00Z