| pubmed-article:9343426 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C0076918 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C0076919 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C0086860 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C0679932 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C1705542 | lld:lifeskim |
| pubmed-article:9343426 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:9343426 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9343426 | pubmed:dateCreated | 1997-11-21 | lld:pubmed |
| pubmed-article:9343426 | pubmed:abstractText | Different mechanisms of transcriptional activation may be required for distinct classes of promoters and cellular conditions. The Epstein-Barr virus (EBV)-encoded transcriptional activator Zta recruits the general transcription factors IID (TFIID) and IIA (TFIIA) to promoter DNA and induces a TATA box-binding protein (TBP)-associated factor-dependent footprint downstream of the transcriptional initiation site. In this study, we investigated the functional significance of TFIID-TFIIA (D-A complex) recruitment by Zta. Alanine substitution mutations in the Zta activation domain which eliminate the ability of Zta to stimulate the D-A complex were examined. These Zta mutants were defective in the ability to activate transcription from an EBV-derived promoter (BHLF1) but activated a highly responsive synthetic promoter (Z7E4T). Both the number of activator binding sites and the core promoter region contribute to the requirement for D-A complex recruitment. These functionally distinct core promoters had significant differences in affinity for TBP and TFIID binding. The D-A complex-recruiting activity of Zta was found to be important for promoter selection in the presence of a competitor template. Conditions which limit TFIID binding to the TATA element or compromise the ability of TFIIA to bind TBP required activator stimulation of the D-A complex. These results indicate that D-A complex recruitment is one of at least two activation pathways utilized by Zta and is the essential pathway for a subset of promoters and conditions which limit TFIID binding to the TATA element. | lld:pubmed |
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| pubmed-article:9343426 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9343426 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9343426 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9343426 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9343426 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9343426 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:9343426 | pubmed:author | pubmed-author:LiebermanP... | lld:pubmed |
| pubmed-article:9343426 | pubmed:author | pubmed-author:OzerJJ | lld:pubmed |
| pubmed-article:9343426 | pubmed:author | pubmed-author:GürselD BDB | lld:pubmed |
| pubmed-article:9343426 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9343426 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:9343426 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9343426 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9343426 | pubmed:pagination | 6624-32 | lld:pubmed |
| pubmed-article:9343426 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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