pubmed-article:3185540 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0035679 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0076919 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0314603 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:3185540 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:3185540 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:3185540 | pubmed:dateCreated | 1988-12-21 | lld:pubmed |
pubmed-article:3185540 | pubmed:abstractText | Selective and accurate transcription of purified genes by RNA polymerase II requires multiple factors. The factor designated TFIID was purified extensively from HeLa cell nuclear extracts by using a simple and novel complementation assay. Thus, TFIID was preferentially inactivated by mild heat treatment of a nuclear extract, and supplementation of the heat-treated extract with TFIID-containing fractions restored adenovirus major late (ML) promoter-dependent transcription. By using this assay, TFIID was purified approximately 300-fold by conventional chromatographic methods. The most purified TFIID fraction was demonstrated to be required for transcription of a number of other cellular and viral class II genes. This factor showed specific interactions with both the adenovirus ML promoter and a human heat shock 70 (hsp-70) promoter. On the ML promoter, the DNase I-protected region extended from around position -40 to position +35, although some discontinuities (and associated hypersensitive sites) were apparent near the initiation site and near position +27; the upstream and downstream boundaries of the TFIID-binding site were also confirmed by exonuclease III digestion experiments. In contrast to these results, the DNase I-protected regions on the human hsp-70 promoter were confined to a smaller area that extended from positions -35 to -19. DNase I hypersensitive sites were observed in both the adenovirus ML and hsp-70 promoters, most notably in the region at position -47. These results indicate either that there are different forms of TFIID or that a single TFIID can interact differently with distinct promoters. | lld:pubmed |
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pubmed-article:3185540 | pubmed:language | eng | lld:pubmed |
pubmed-article:3185540 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3185540 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3185540 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3185540 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:3185540 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3185540 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3185540 | pubmed:month | Oct | lld:pubmed |
pubmed-article:3185540 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:3185540 | pubmed:author | pubmed-author:NakajimaNN | lld:pubmed |
pubmed-article:3185540 | pubmed:author | pubmed-author:RoederR GRG | lld:pubmed |
pubmed-article:3185540 | pubmed:author | pubmed-author:HorikoshiMM | lld:pubmed |
pubmed-article:3185540 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3185540 | pubmed:volume | 8 | lld:pubmed |