| http://purl.uniprot.org/citations/12379856 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12379856 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12379856 | http://www.w3.org/2000/01/rdf-schema#comment | "The Sir3 protein helps form telomeric heterochromatin by interacting with hypoacetylated histone H4 lysine 16 (H4-Lys16). The molecular nature of the heterochromatin boundary is still unknown. Here we show that the MYST-like acetyltransferase Sas2p is required for the acetylation (Ac) of H4-Lys16 in euchromatin. In a sas2Delta strain or a phenocopy Lys16Arg mutant, Sir3p spreads from roughly 3 kb to roughly 15 kb, causing hypoacetylation and repression of adjacent chromatin. We also found that disruption of Sir3p binding in a deacetylase-deficient Sir 2Delta strain can be suppressed by sas2Delta. These data indicate that opposing effects of Sir2p and Sas2p on acetylation of H4-Lys16 maintain the boundary at telomeric heterochromatin."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.org/dc/terms/identifier | "doi:10.1038/ng1017"xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.org/dc/terms/identifier | "doi:10.1038/ng1017"xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/author | "Grunstein M."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/author | "Grunstein M."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/author | "Luo K."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/author | "Luo K."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/author | "Suka N."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/author | "Suka N."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/name | "Nat. Genet."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/name | "Nat. Genet."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/pages | "378-383"xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/pages | "378-383"xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/title | "Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/title | "Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin."xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/volume | "32"xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://purl.uniprot.org/core/volume | "32"xsd:string |
| http://purl.uniprot.org/citations/12379856 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12379856 |
| http://purl.uniprot.org/citations/12379856 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12379856 |
| http://purl.uniprot.org/citations/12379856 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12379856 |
| http://purl.uniprot.org/citations/12379856 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12379856 |