TFIIA regulates TBP and TFIID dimers

被引：37

作者：

Coleman, RA ^{[1
]}

Taggart, AKP ^{[1
]}

Burma, S ^{[1
]}

Chicca, JJ ^{[1
]}

Pugh, BF ^{[1
]}

机构：

[1] Penn State Univ, Dept Biochem & Mol Biol, Ctr Gene Regulat, University Pk, PA 16802 USA

来源：

MOLECULAR CELL | 1999年 / 4卷 / 03期

关键词：

D O I：

10.1016/S1097-2765(00)80453-0

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：

Dimerization of the TATA-binding protein (TBP) through its DNA-binding domain blocks TBP from accessing DNA and prevents unregulated gene expression. TFIIA plays a central role in loading TBP and its multisubunit counterpart TFIID onto promoter DNA, and it is therefore a candidate for regulating TBP/TFIID dimerization. Here, we show that TFIIA promotes the dissociation of TBP dimers directly and in doing so accelerates the kinetics of DNA binding. TFIID dimer dissociation was found to be slow and rate limiting in DNA binding. TFIIA induced a rapid dissociation of TFIID dimers, allowing TFIID to readily load onto promoter DNA. Together, these results suggest a novel mechanism by which TFIIA assists in regulating gene expression.

引用

页码：451 / 457

页数：7

共 34 条

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