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http://purl.uniprot.org/citations/14536086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14536086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14536086http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/14536086http://www.w3.org/2000/01/rdf-schema#comment"Methylation of histone tails plays an important role in chromatin structure and function. Previously, we reported that ESET/SETDB1 is a histone methyltransferase (HMTase). Here, we show that SETDB1 tightly associates with the human homolog of mAM, a murine ATFa-associated factor. Although recombinant ESET can methylate lysine 9 of histone H3 (H3-K9), its activity is severely compromised when compared to that of the ESET/mAM complex. mAM stimulates ESET enzymatic activity by increasing the Vmax and decreasing the Km. Importantly, mAM facilitates the ESET-dependent conversion of dimethyl H3-K9 to the trimethyl state both in vitro and in vivo. Chromatin-based transcription and ChIP analyses demonstrate that mAM enhances ESET-mediated transcriptional repression in a SAM-dependent manner, and this repression correlates with H3-K9 trimethylation at the promoter. Thus, our studies establish that promoter H3-K9 trimethylation is the cause of transcriptional repression and that mAM/hAM facilitates conversion of H3-K9 dimethyl to trimethyl by ESET/SETDB1."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2003.08.007"xsd:string
http://purl.uniprot.org/citations/14536086http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2003.08.007"xsd:string
http://purl.uniprot.org/citations/14536086http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2003.08.007"xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Xia L."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Xia L."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Tempst P."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Tempst P."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Erdjument-Bromage H."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Erdjument-Bromage H."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Cao R."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Cao R."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Chatton B."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Chatton B."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Roeder R.G."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"Roeder R.G."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"An W."xsd:string
http://purl.uniprot.org/citations/14536086http://purl.uniprot.org/core/author"An W."xsd:string