http://purl.uniprot.org/citations/16543222 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16543222 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16543222 | http://www.w3.org/2000/01/rdf-schema#comment | "SWR1-Com, which is responsible for depositing H2A.Z into chromatin, shares four subunits with the NuA4 histone acetyltransferase complex. This overlap in composition led us to test whether H2A.Z was a substrate of NuA4 in vitro and in vivo. The N-terminal tail of H2A.Z was acetylated in vivo at multiple sites by a combination of NuA4 and SAGA. H2A.Z acetylation was also dependent on SWR1-Com, causing H2A.Z to be efficiently acetylated only when incorporated in chromatin. Unacetylatable H2A.Z mutants were, like wild-type H2A.Z, enriched at heterochromatin boundaries, but were unable to block spreading of heterochromatin. A mutant version of H2A.Z that could not be acetylated, in combination with a mutation in a nonessential gene in the NuA4 complex, caused a pronounced decrease in growth rate. This H2A.Z mutation was lethal in combination with a mutant version of histone H4 that could not be acetylated by NuA4. Taken together, these results show a role for H2A.Z acetylation in restricting silent chromatin, and reveal that acetylation of H2A.Z and H4 can contribute to a common function essential to life."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.org/dc/terms/identifier | "doi:10.1101/gad.1386306"xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.org/dc/terms/identifier | "doi:10.1101/gad.1386306"xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/author | "Rine J."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/author | "Rine J."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/author | "Babiarz J.E."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/author | "Babiarz J.E."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/author | "Halley J.E."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/author | "Halley J.E."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/name | "Genes Dev."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/name | "Genes Dev."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/pages | "700-710"xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/pages | "700-710"xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/title | "Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/title | "Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae."xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/volume | "20"xsd:string |
http://purl.uniprot.org/citations/16543222 | http://purl.uniprot.org/core/volume | "20"xsd:string |
http://purl.uniprot.org/citations/16543222 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16543222 |
http://purl.uniprot.org/citations/16543222 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16543222 |
http://purl.uniprot.org/citations/16543222 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16543222 |
http://purl.uniprot.org/citations/16543222 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16543222 |