| pubmed-article:1986253 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C0076919 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:1986253 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:1986253 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1986253 | pubmed:dateCreated | 1991-2-14 | lld:pubmed |
| pubmed-article:1986253 | pubmed:abstractText | Transcription factor IID from Saccharomyces cerevisiae (YIID) binds the TATA box element present in most RNA polymerase II promoters. In this work, partial proteolysis was used as a biochemical probe of YIID structure. YIID consists of a protease-sensitive amino terminus and a highly stable, protease-resistant carboxy-terminal core. The cleavage sites of the predominant chymotrypsin- and trypsin-derived fragments were mapped to amino acid residues 40 to 41 and 48 to 49, respectively, by amino-terminal peptide sequencing. Removal of the amino terminus resulted in a dramatic increase in the ability of YIID to form a stable complex with DNA during gel electrophoresis mobility shift assays and a two- to fourfold increase in DNA-binding affinity, as assayed by DNase I footprinting analysis. The carboxy-terminal 190-amino-acid core was competent for transcription in vitro and was similar in activity to native YIID. DNA containing a TATA element induced hypersensitive sites in the amino-terminal domain and stabilized the core domain to further proteolytic attack. Native YIID did not bind to a TATA box at 0 degrees C, whereas the carboxy-terminal DNA-binding domain did. These results suggest that YIID undergoes a conformational change upon binding to a TATA box. Southern blotting showed that the carboxy-terminal domain is highly conserved, while the amino-terminal domain diverged rapidly in evolution, even between closely related budding yeasts. | lld:pubmed |
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| pubmed-article:1986253 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1986253 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1986253 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1986253 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1986253 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1986253 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1986253 | pubmed:author | pubmed-author:KaoC CCC | lld:pubmed |
| pubmed-article:1986253 | pubmed:author | pubmed-author:BerkA JAJ | lld:pubmed |
| pubmed-article:1986253 | pubmed:author | pubmed-author:SchmidtM CMC | lld:pubmed |
| pubmed-article:1986253 | pubmed:author | pubmed-author:LiebermanP... | lld:pubmed |
| pubmed-article:1986253 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1986253 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1986253 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1986253 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1986253 | pubmed:pagination | 63-74 | lld:pubmed |
| pubmed-article:1986253 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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