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The acidic transcriptional activator GAL‐VP16 acts on preformed template‐committed complexes.
Author(s) -
White J.,
Brou C.,
Wu J.,
Lutz Y.,
Moncollin V.,
Chambon P.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05282.x
Subject(s) - biology , activator (genetics) , biochemistry , microbiology and biotechnology , gene
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.