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http://purl.uniprot.org/citations/12398767http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12398767http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12398767http://www.w3.org/2000/01/rdf-schema#comment"Covalent modifications of histone tails play important roles in gene transcription and silencing. We recently identified an ERG ( ets -related gene)-associated protein with a SET (suppressor of variegation, enhancer of zest and trithorax) domain (ESET) that was found to have the activity of a histone H3-specific methyltransferase. In the present study, we investigated the interaction of ESET with other chromatin remodelling factors. We show that ESET histone methyltransferase associates with histone deacetylase 1 (HDAC1) and HDAC2, and that ESET also interacts with the transcription co-repressors mSin3A and mSin3B. Deletion analysis of ESET reveals that an N-terminal region containing a tudor domain is responsible for interaction with mSin3A/B and association with HDAC1/2, and that truncation of ESET enhances its binding to mSin3. When bound to a promoter, ESET represses the transcription of a downstream luciferase reporter gene. This repression by ESET is independent of its histone methyltransferase activity, but correlates with its binding to the mSin3 co-repressors. In addition, the repression can be partially reversed by treatment with the HDAC inhibitor trichostatin A. Taken together, these data suggest that ESET histone methyltransferase can form a large, multi-protein complex(es) with mSin3A/B co-repressors and HDAC1/2 that participates in multiple pathways of transcriptional repression."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.org/dc/terms/identifier"doi:10.1042/bj20020854"xsd:string
http://purl.uniprot.org/citations/12398767http://purl.org/dc/terms/identifier"doi:10.1042/bj20020854"xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Yang L."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Yang L."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Matsui Y."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Matsui Y."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Chansky H.A."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Chansky H.A."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Taborsky G.J. Jr."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Taborsky G.J. Jr."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Benedetti D."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Benedetti D."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Blackburn M.L."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Blackburn M.L."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Krumm A.A."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Krumm A.A."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Mei Q."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Mei Q."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Zielinska-Kwiatkowska A."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/author"Zielinska-Kwiatkowska A."xsd:string
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12398767http://purl.uniprot.org/core/date"2003"xsd:gYear