pubmed-article:11390659 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11390659 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:11390659 | lifeskim:mentions | umls-concept:C0292369 | lld:lifeskim |
pubmed-article:11390659 | lifeskim:mentions | umls-concept:C1156210 | lld:lifeskim |
pubmed-article:11390659 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:11390659 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:11390659 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:11390659 | pubmed:dateCreated | 2001-6-6 | lld:pubmed |
pubmed-article:11390659 | pubmed:abstractText | Snf-Swi, the prototypical ATP-dependent nucleosome-remodeling complex, regulates transcription of a subset of yeast genes. With the exception of Snf2p, the ATPase subunit, the functions of the other components are unknown. We have investigated the role of the conserved Snf-Swi core subunit Snf5p through characterization of two conditional snf5 mutants. The mutants contain single amino acid alterations of invariant or conserved residues that abolish Snf-Swi-dependent transcription by distinct mechanisms. One mutation impairs Snf-Swi assembly and, consequently, its stable association with a target promoter. The other blocks a postrecruitment catalytic remodeling step. These findings suggest that Snf5p coordinates the assembly and nucleosome-remodeling activities of Snf-Swi. | lld:pubmed |
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pubmed-article:11390659 | pubmed:language | eng | lld:pubmed |
pubmed-article:11390659 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11390659 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11390659 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11390659 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11390659 | pubmed:month | Jul | lld:pubmed |
pubmed-article:11390659 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:11390659 | pubmed:author | pubmed-author:CamGG | lld:pubmed |