THE ACIDIC TRANSCRIPTIONAL ACTIVATOR GAL-VP16 ACTS ON PREFORMED TEMPLATE-COMMITTED COMPLEXES

被引：113

作者：

WHITE, J ^{[1
]}

BROU, C ^{[1
]}

WU, J ^{[1
]}

LUTZ, Y ^{[1
]}

MONCOLLIN, V ^{[1
]}

CHAMBON, P ^{[1
]}

机构：

[1] FAC MED STRASBOURG,INST CHIM BIOL,GENET MOLEC EUCARYOTES LAB,CNRS,INSERM,F-67085 STRASBOURG,FRANCE

来源：

EMBO JOURNAL | 1992年 / 11卷 / 06期

关键词：

INHIBITION OF GAL-VP16; TFIIB; TFIID; TRANSCRIPTIONAL ENHANCER; VP16; ANTIBODIES;

D O I：

10.1002/j.1460-2075.1992.tb05282.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 its 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.

引用

页码：2229 / 2240

页数：12

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