期刊
SCIENCE
卷 328, 期 5977, 页码 501-504出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1184953
关键词
-
资金
- Deutsche Forschungsgemeinschaft [Ro617/16-1, Wa1126/3-1, NSF MCB-0744422]
- NIH [GM037219]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0744422] Funding Source: National Science Foundation
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据