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http://purl.uniprot.org/citations/24396869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24396869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24396869http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/24396869http://www.w3.org/2000/01/rdf-schema#comment"SUV420H1 and SUV420H2 are two highly homologous enzymes that methylate lysine 20 of histone H4 (H4K20), a mark that has been implicated in transcriptional regulation. In this study, we present the high-resolution crystal structures of human SUV420H1 and SUV420H2 in complex with SAM, and report their substrate specificity. Both methyltransferases have a unique N-terminal domain and Zn-binding post-SET domain, and prefer the monomethylated histone H4K20 as a substrate in vitro. No histone H4K20 trimethylation activity was detected by our radioactivity-based assay for either enzyme, consistent with the presence of a conserved serine residue that forms a hydrogen bond with the target lysine side-chain and limits the methylation level."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2013.10.020"xsd:string
http://purl.uniprot.org/citations/24396869http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2013.10.020"xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Wu H."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Wu H."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Zeng H."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Zeng H."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Dong A."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Dong A."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Vedadi M."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Vedadi M."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Schapira M."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Schapira M."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Lam R."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Lam R."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Wu X.H."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Wu X.H."xsd:string
http://purl.uniprot.org/citations/24396869http://purl.uniprot.org/core/author"Siarheyeva A."xsd:string