A NusE:NusG Complex Links Transcription and Translation

被引：264

作者：

Burmann, Bjoern M. ^{[1
,2
]}

Schweimer, Kristian ^{[1
,2
]}

Luo, Xiao ^{[3
]}

Wahl, Markus C. ^{[3
]}

Stitt, Barbara L. ^{[4
,5
]}

Gottesman, Max E. ^{[6
,7
]}

Roesch, Paul ^{[1
,2
]}

机构：

[1] Univ Bayreuth, Lehrstuhl Biopolymere, D-95447 Bayreuth, Germany

[2] Univ Bayreuth, Forschungszentrum BioMakromol, D-95447 Bayreuth, Germany

[3] Free Univ Berlin, Fachbereich Biol Chem Pharm, Inst Chem & Biochem, AG Strukturbiochem, D-14195 Berlin, Germany

[4] Temple Univ, Sch Med, Dept Biochem, Philadelphia, PA 19140 USA

[5] Temple Univ, Sch Med, Fels Inst Canc Res & Mol Biol, Philadelphia, PA 19140 USA

[6] Columbia Univ, Dept Microbiol, Med Ctr, New York, NY 10032 USA

[7] Columbia Univ, Inst Canc Res, Med Ctr, New York, NY 10032 USA

来源：

SCIENCE | 2010年 / 328卷 / 5977期

基金：

美国国家科学基金会;

关键词：

ESCHERICHIA-COLI; ANTITERMINATION COMPLEX; RNA-TRANSCRIPTION; PHAGE-LAMBDA; FACTOR-NUSG; N-PROTEIN; BOXA RNA; ELONGATION; TERMINATION; RHO;

D O I：

10.1126/science.1184953

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Bacterial NusG is a highly conserved transcription factor that is required for most Rho activity in vivo. We show by nuclear magnetic resonance spectroscopy that Escherichia coli NusG carboxy-terminal domain forms a complex alternatively with Rho or with transcription factor NusE, a protein identical to 30S ribosomal protein S10. Because NusG amino-terminal domain contacts RNA polymerase and the NusG carboxyl-terminal domain interaction site of NusE is accessible in the ribosomal 30S subunit, NusG may act as a link between transcription and translation. Uncoupling of transcription and translation at the ends of bacterial operons enables transcription termination by Rho factor, and competition between ribosomal NusE and Rho for NusG helps to explain why Rho cannot terminate translated transcripts.

引用

页码：501 / 504

页数：4

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