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http://purl.uniprot.org/citations/11283354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11283354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11283354http://www.w3.org/2000/01/rdf-schema#comment"The assembly of higher order chromatin structures has been linked to the covalent modifications of histone tails. We provide in vivo evidence that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast. Both the conserved chromo- and SET domains of Clr4 are required for H3 Lys9 methylation in vivo. Localization of Swi6, a homolog of Drosophila HP1, to heterochomatic regions is dependent on H3 Lys9 methylation. Moreover, an H3-specific deacetylase Clr3 and a beta-propeller domain protein Rik1 are required for H3 Lys9 methylation by Clr4 and Swi6 localization. These data define a conserved pathway wherein sequential histone modifications establish a "histone code" essential for the epigenetic inheritance of heterochromatin assembly."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.org/dc/terms/identifier"doi:10.1126/science.1060118"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.org/dc/terms/identifier"doi:10.1126/science.1060118"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Nakayama J."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Nakayama J."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Strahl B.D."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Strahl B.D."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Grewal S.I.S."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Grewal S.I.S."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Rice J.C."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/author"Rice J.C."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/pages"110-113"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/pages"110-113"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/title"Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/title"Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly."xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/volume"292"xsd:string
http://purl.uniprot.org/citations/11283354http://purl.uniprot.org/core/volume"292"xsd:string