http://purl.uniprot.org/citations/12845608 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12845608 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12845608 | http://www.w3.org/2000/01/rdf-schema#comment | "Several homologues of the Drosophila Su(var)3-9 protein were recently reported to methylate lysine 9 of histone H3. Whereas this methylation signal served to recruit heterochromatin-associated proteins to transcriptionally silenced regions, histone H3 methylated at lysine 4 was associated with transcriptionally active areas of the genome. These findings suggested that the interplay between lysine 4 and 9 methylation is crucial in eukaryotic gene regulation. Here we provide evidence that Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3. In addition, we show that the absence of Set1p and lysine 4 methylation result in decreased transcription of approximately 80% of the genes in S. cerevisiae. Hierarchical clustering analysis of the set1(-) expression profile revealed a correspondence to that of a mad2(-) strain, suggesting that the transcriptional defect in the set1(-) strain may be due to changes in chromatin structure. These findings establish a central role for methylation of histone H3 lysine 4 in transcriptional regulation."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.org/dc/terms/identifier | "doi:10.1002/yea.995"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.org/dc/terms/identifier | "doi:10.1002/yea.995"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/author | "Boa S."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/author | "Boa S."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/author | "Coert C."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/author | "Coert C."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/author | "Patterton H.-G."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/author | "Patterton H.-G."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/name | "Yeast"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/name | "Yeast"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/pages | "827-835"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/pages | "827-835"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/title | "Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/title | "Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine 4 of histone H3 and is required for efficient gene expression."xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/volume | "20"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://purl.uniprot.org/core/volume | "20"xsd:string |
http://purl.uniprot.org/citations/12845608 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12845608 |
http://purl.uniprot.org/citations/12845608 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12845608 |
http://purl.uniprot.org/citations/12845608 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12845608 |
http://purl.uniprot.org/citations/12845608 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12845608 |