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http://purl.uniprot.org/citations/12077605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12077605http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12077605http://www.w3.org/2000/01/rdf-schema#comment"In eukaryotes, the DNA of the genome is packaged with histone proteins to form nucleosomal filaments, which are, in turn, folded into a series of less well understood chromatin structures. Post-translational modifications of histone tail domains modulate chromatin structure and gene expression. Of these, histone ubiquitination is poorly understood. Here we show that the ubiquitin-conjugating enzyme Rad6 (Ubc2) mediates methylation of histone H3 at lysine 4 (Lys 4) through ubiquitination of H2B at Lys 123 in yeast (Saccharomyces cerevisiae). Moreover, H3 (Lys 4) methylation is abolished in the H2B-K123R mutant, whereas H3-K4R retains H2B (Lys 123) ubiquitination. These data indicate a unidirectional regulatory pathway in which ubiquitination of H2B (Lys 123) is a prerequisite for H3 (Lys 4) methylation. We also show that an H2B-K123R mutation perturbs silencing at the telomere, providing functional links between Rad6-mediated H2B (Lys 123) ubiquitination, Set1-mediated H3 (Lys 4) methylation, and transcriptional silencing. Thus, these data reveal a pathway leading to gene regulation through concerted histone modifications on distinct histone tails. We refer to this as 'trans-tail' regulation of histone modification, a stated prediction of the histone code hypothesis."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.org/dc/terms/identifier"doi:10.1038/nature00883"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.org/dc/terms/identifier"doi:10.1038/nature00883"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/author"Allis C.D."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/author"Sun Z.-W."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/author"Sun Z.-W."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/pages"104-108"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/pages"104-108"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/title"Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/title"Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast."xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/volume"418"xsd:string
http://purl.uniprot.org/citations/12077605http://purl.uniprot.org/core/volume"418"xsd:string
http://purl.uniprot.org/citations/12077605http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12077605
http://purl.uniprot.org/citations/12077605http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12077605
http://purl.uniprot.org/citations/12077605http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12077605
http://purl.uniprot.org/citations/12077605http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12077605
http://purl.uniprot.org/uniprot/P06104http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12077605
http://purl.uniprot.org/uniprot/P06104#attribution-CA0F24FA0ACD0A269AACAC357C15247Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12077605