Diffusion-controlled DNA recognition by an unfolded, monomeric bZIP transcription factor

被引：46

作者：

Berger, C ^{[1
]}

Piubelli, L ^{[1
]}

Haditsch, U ^{[1
]}

Bosshard, HR ^{[1
]}

机构：

[1] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland

来源：

FEBS LETTERS | 1998年 / 425卷 / 01期

关键词：

protein-DNA recognition; kinetic mechanism; transcription factor GCN4; monomer-dimer equilibrium; fluorescence-labeled DNA;

D O I：

10.1016/S0014-5793(98)00156-2

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：

Basic leucine zipper (bZIP) transcription factors are diners that recognize mainly palindromic DNA sites. It has been assumed that bZIP factors have to form a dimer in order to bind to their target DNA, We find that DNA binding of both monomeric and dimeric bZIP transcription factor GCN4 is diffusion-limited and that, therefore, the rate of dimerization of the bZIP domain does not affect the rate of DNA recognition and GCN4 need not dimerize in order to bind to its specific DNA site, The results have implications for the mechanism by which bZIP transcription factors find their target sites for transcriptional regulation, (C) 1998 Federation of European Biochemical Societies.

引用

页码：14 / 18

页数：5

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