The conformation of the transcription factor TFIIB modulates the response to transcriptional activators in vivo

被引：26

作者：

Hawkes, NA ^{[1
]}

Evans, R ^{[1
]}

Roberts, SGE ^{[1
]}

机构：

[1] Univ Dundee, Div Gene Express, Dept Biochem, Wellcome Trust Bioctr, Dundee DD1 5EH, Scotland

来源：

CURRENT BIOLOGY | 2000年 / 10卷 / 05期

基金：

英国惠康基金;

关键词：

D O I：

10.1016/S0960-9822(00)00363-8

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 general transcription factor TFIIB plays a crucial role in the assembly of the transcriptional preinitiation complex and has also been proposed as a target of transcriptional activator proteins (reviewed in [1]). TFIIB is composed of two domains which are engaged in an intramolecular interaction that is disrupted upon interaction with the activation domain of the Herpesvirus VP16 protein in vitro [2,3], The significance of this event for transcriptional activation is not known, however. The amino-terminal intramolecular interaction domain is the most conserved region of TFIIB and plays a role in transcription start-site selection [4-6]. in addition, we have shown previously that the integrity of this region is required for transcriptional activation in vivo [4], Here, we have defined a charge cluster at the amino terminus of TFIIB that is required for transcriptional activation in vivo. We found that this domain determines the affinity of the TFIIB intramolecular interaction and the ability of TFIIB to interact with a transcriptional activation domain, but not with components of the holoenzyme, Our results suggest that the intramolecular interaction in TFIIB regulates transcriptional activation in vivo.

引用

页码：273 / 276

页数：4

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