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http://purl.uniprot.org/citations/18264113http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18264113http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18264113http://www.w3.org/2000/01/rdf-schema#comment"Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.1384"xsd:string
http://purl.uniprot.org/citations/18264113http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.1384"xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Cheng X."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Cheng X."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Horton J.R."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Horton J.R."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Lee D.Y."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Lee D.Y."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Stallcup M.R."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Stallcup M.R."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Collins R.E."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Collins R.E."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Northrop J.P."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/author"Northrop J.P."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/pages"245-250"xsd:string
http://purl.uniprot.org/citations/18264113http://purl.uniprot.org/core/pages"245-250"xsd:string