Structural Basis for NusA Stabilized Transcriptional Pausing

被引：128

作者：

Guo, Xieyang ^{[1
,2
,3
,4
]}

Myasnikov, Alexander G. ^{[1
,2
,3
,4
,6
]}

Chen, James ^{[5
]}

Crucifix, Corinne ^{[1
,2
,3
,4
]}

Papai, Gabor ^{[1
,2
,3
,4
]}

Takacs, Maria ^{[1
,2
,3
,4
]}

Schultz, Patrick ^{[1
,2
,3
,4
]}

Weixlbaumer, Albert ^{[1
,2
,3
,4
]}

机构：

[1] IGBMC, Dept Integrated Struct Biol, F-67404 Illkirch Graffenstaden, France

[2] Univ Strasbourg, F-67404 Illkirch Graffenstaden, France

[3] CNRS, UMR 7104, F-67404 Illkirch Graffenstaden, France

[4] INSERM, U964, F-67404 Illkirch Graffenstaden, France

[5] Rockefeller Univ, 1230 York Ave, New York, NY 10065 USA

[6] Univ Calif San Francisco, San Francisco, CA 94158 USA

来源：

MOLECULAR CELL | 2018年 / 69卷 / 05期

基金：

欧洲研究理事会;

关键词：

BACTERIAL RNA-POLYMERASE; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE; ALPHA-SUBUNIT; EXIT CHANNEL; BINDING; SITE; DNA; TERMINATION; REVEALS;

D O I：

10.1016/j.molcel.2018.02.008

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：

Transcriptional pausing by RNA polymerases (RNAPs) is a key mechanism to regulate gene expression in all kingdoms of life and is a prerequisite for transcription termination. The essential bacterial transcription factor NusA stimulates both pausing and termination of transcription, thus playing a central role. Here, wereport single-particle electron cryo-microscopy reconstructions of NusA bound to paused E. coli RNAP elongation complexes with and without a pause-enhancing hairpin in the RNA exit channel. The structures reveal four interactions between NusA and RNAP that suggest how NusA stimulates RNA folding, pausing, and termination. An asymmetric translocation intermediate of RNA and DNA converts the active site of the enzyme into an inactive state, providing a structural explanation for the inhibition of catalysis. Comparing RNAP at different stages of pausing provides insights on the dynamic nature of the process and the role of NusA as a regulatory factor.

引用

页码：816 / +

页数：16