pubmed-article:15598821 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15598821 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:15598821 | lifeskim:mentions | umls-concept:C0035143 | lld:lifeskim |
pubmed-article:15598821 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:15598821 | lifeskim:mentions | umls-concept:C0242617 | lld:lifeskim |
pubmed-article:15598821 | lifeskim:mentions | umls-concept:C1417038 | lld:lifeskim |
pubmed-article:15598821 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:15598821 | pubmed:dateCreated | 2004-12-15 | lld:pubmed |
pubmed-article:15598821 | pubmed:abstractText | The HO gene in Saccharomyces cerevisiae is regulated by a large and complex promoter that is similar to promoters in higher order eukaryotes. Within this promoter are 10 potential binding sites for the a1-alpha2 heterodimer, which represses HO and other haploid-specific genes in diploid yeast cells. We have determined that a1-alpha2 binds to these sites with differing affinity, and that while certain strong-affinity sites are crucial for repression of HO, some of the weak-affinity sites are dispensable. However, these weak-affinity a1-alpha2-binding sites are strongly conserved in related yeast species and have a role in maintaining repression upon the loss of strong-affinity sites. We found that these weak sites are sufficient for a1-alpha2 to partially repress HO and recruit the Tup1-Cyc8 (Tup1-Ssn6) co-repressor complex to the HO promoter. We demonstrate that the Swi5 activator protein is not bound to URS1 in diploid cells, suggesting that recruitment of the Tup1-Cyc8 complex by a1-alpha2 prevents DNA binding by activator proteins resulting in repression of HO. | lld:pubmed |
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pubmed-article:15598821 | pubmed:language | eng | lld:pubmed |
pubmed-article:15598821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15598821 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15598821 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15598821 | pubmed:issn | 1362-4962 | lld:pubmed |
pubmed-article:15598821 | pubmed:author | pubmed-author:MathiasJonath... | lld:pubmed |
pubmed-article:15598821 | pubmed:author | pubmed-author:VershonAndrew... | lld:pubmed |
pubmed-article:15598821 | pubmed:author | pubmed-author:SenguptaAnirv... | lld:pubmed |
pubmed-article:15598821 | pubmed:author | pubmed-author:HanlonSean... | lld:pubmed |
pubmed-article:15598821 | pubmed:author | pubmed-author:O'FlanaganRua... | lld:pubmed |
pubmed-article:15598821 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:15598821 | pubmed:volume | 32 | lld:pubmed |
pubmed-article:15598821 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15598821 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15598821 | pubmed:pagination | 6469-78 | lld:pubmed |
pubmed-article:15598821 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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