| Literature DB >> 1376247 |
J White1, C Brou, J Wu, Y Lutz, V Moncollin, P Chambon.
Abstract
The action of the chimeric acidic transcriptional activator GAL-VP16 has been investigated by performing a series of kinetic experiments using the detergent Sarkosyl as well as monoclonal antibodies which specifically inhibit GAL-VP16 DNA binding and transcriptional activation. GAL-VP16 binds to recognition site rapidly, remains bound after transcriptional initiation and is required to maintain stimulated levels of reinitiation. GAL-VP16 action, which appears to result in an increase in the number of preinitiation complexes formed, occurs after the formation of template-committed complexes composed of promoter-bound TFIIA (STF) and a partially purified TFIID fraction conferring GAL-VP16 responsiveness on a reconstituted basal transcription system. This TFIID fraction cannot be replaced by TFIIB or cloned TFIID. Our results suggest that GAL-VP16 activates step(s) in preinitiation complex assembly occurring after TFIID has bound.Entities:
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Year: 1992 PMID: 1376247 PMCID: PMC556690 DOI: 10.1002/j.1460-2075.1992.tb05282.x
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598