Organization of an Activator-Bound RNA Polymerase Holoenzyme

被引：61

作者：

Bose, Daniel ^{[1
]}

Pape, Tillmann ^{[1
]}

Burrows, Patricia C. ^{[2
]}

Rappas, Mathieu ^{[1
]}

Wigneshweraraj, Siva R. ^{[3
]}

Buck, Martin ^{[2
]}

Zhang, Xiaodong ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Fac Nat Sci, Dept Life Sci, Struct Biol Ctr,Div Mol Biosci, London SW7 2AZ, England

[2] Univ London Imperial Coll Sci Technol & Med, Fac Nat Sci, Dept Life Sci, Div Biol, London SW7 2AZ, England

[3] Univ London Imperial Coll Sci Technol & Med, Fac Med, Dept Microbiol, Div Invest Sci, London SW7 2AZ, England

来源：

MOLECULAR CELL | 2008年 / 32卷 / 03期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/j.molcel.2008.09.015

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：

Transcription initiation involves the conversion from closed promoter complexes, comprising RNA polymerase (RNAP) and double-stranded promoter DNA, to open complexes, in which the enzyme is able to access the DNA template in a single-stranded form. The complex between bacterial RNAP and its major variant sigma factor sigma(54) remains as a closed complex until ATP hydrolysis-dependent remodeling by activator proteins occurs. This remodeling facilitates DNA melting and allows the transition to the open complex. Here we present cryoelectron microscopy reconstructions of bacterial RNAP in complex with 654 alone, and of RNAP-sigma(54) with an AAA+ activator. Together with photo-crosslinking data that establish the location of promoter DNA within the complexes, we explain why the RNAP-sigma(54) closed complex is unable to access the DNA template and propose how the structural changes induced by activator binding can initiate conformational changes that ultimately result in formation of the open complex.

引用

页码：337 / 346

页数：10

共 59 条

[1] Structural basis for converting a general transcription factor into an operon-specific virulence regulator [J].