| http://purl.uniprot.org/citations/26182431 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26182431 | http://www.w3.org/2000/01/rdf-schema#comment | "Chromatin structure is implicated in regulating gene transcription in stress response. Transcription factors, transferases and deacetylases, such as multicopy suppressor of SNF1 protein 2 (Msn2), SET domain-containing protein 1 (Set1) and sucrose NonFermenting protein 1 (Snf1), have been identified as key regulators in stress response. In the present study, we reported the dynamics of nucleosome occupancy, Histone Two A Z1 (Htz1) deposition and histone H3 lysine 4 dimethylation (H3K4me2) and histone H3 lysine 79 trimethylation (H3K79me3) in Saccharomyces cerevisiae under oleate stress. Our results indicated that citrate cycle-associated genes are enhanced and ribosome genes are repressed during the glucose-oleate shift. Importantly, Htz1 acts as a sensor for oleate stress. High-throughput ChIP-chip analysis showed that Htz1 has redistributed across the genome during oleate stress. The number of Htz1-bound genes increases with stress and the number of Htz1-bound ribosome genes decreases with stress. The dynamics of Htz1 and H3K79me3 around transcription factor-binding sites correlate with transcriptional changes. Moreover, we found that nucleosome dynamics are coupled with Htz1 binding changes upon stress. In unstressed conditions (2% glucose), nucleosome occupancy is comparable between Htz1-bound genes and Htz1-depleted genes; in stressed conditions (0.2% oleate for 8 h), the nucleosome occupancy of Htz1-depleted genes is significantly lower than that of Htz1-bound genes. We also found that Msn2 acts an important role in response to the oleate stress and Htz1 is dynamic in Msn2-target genes. Htz1 senses the oleate stress and undergoes a global redistribution and this change couples dynamics of nucleosome occupancy. Our analysis suggests that Htz1 and nucleosome dynamics change in response to oleate stress."xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.org/dc/terms/identifier | "doi:10.1042/bsr20150114"xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/author | "Liu H."xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/author | "Li G."xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/author | "Liu L."xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/author | "Wan Y."xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/name | "Biosci Rep"xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/pages | "e00224"xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/title | "Functional role of histone variant Htz1 in the stress response to oleate in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://purl.uniprot.org/core/volume | "35"xsd:string |
| http://purl.uniprot.org/citations/26182431 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26182431 |
| http://purl.uniprot.org/citations/26182431 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26182431 |
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| http://purl.uniprot.org/uniprot/#_Q12692-mappedCitation-26182431 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26182431 |
| http://purl.uniprot.org/uniprot/P61830 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26182431 |
| http://purl.uniprot.org/uniprot/P33748 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26182431 |
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| http://purl.uniprot.org/uniprot/Q12692 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26182431 |