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http://purl.uniprot.org/citations/20208542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20208542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20208542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/20208542http://www.w3.org/2000/01/rdf-schema#comment"Histone lysine methylation is dynamically regulated by lysine methyltransferases and lysine demethylases. Here we show that PHD finger protein 8 (PHF8), a protein containing a PHD finger and a Jumonji C (JmjC) domain, is associated with hypomethylated rRNA genes (rDNA). PHF8 interacts with the RNA polymerase I transcription machinery and with WD repeat-containing protein 5 (WDR5)-containing H3K4 methyltransferase complexes. PHF8 exerts a positive effect on rDNA transcription, with transcriptional activation requiring both the JmjC domain and the PHD finger. PHF8 demethylates H3K9me1/2, and its catalytic activity is stimulated by adjacent H3K4me3. A point mutation within the JmjC domain that is linked to mental retardation with cleft lip and palate (XLMR-CL/P) abolishes demethylase activity and transcriptional activation. Though further work is needed to unravel the contribution of PHF8 activity to mental retardation and cleft lip/palate, our results reveal a functional interplay between H3K4 methylation and H3K9me1/2 demethylation, linking dynamic histone methylation to rDNA transcription and neural disease."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.1778"xsd:string
http://purl.uniprot.org/citations/20208542http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.1778"xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Ye J."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Ye J."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Feng W."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Feng W."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Jenuwein T."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Jenuwein T."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Grummt I."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Grummt I."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Yonezawa M."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/author"Yonezawa M."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/pages"445-450"xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/pages"445-450"xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/title"PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/title"PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation."xsd:string
http://purl.uniprot.org/citations/20208542http://purl.uniprot.org/core/volume"17"xsd:string