Structural basis of Q-dependent transcription antitermination

Jing Shi, Xiang Gao, Tongguan Tian, Zhaoyang Yu, Bo Gao, Aijia Wen, Linlin You, Shenghai Chang, Xing Zhang, Yu Zhang and Yu Feng ()
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Jing Shi: Zhejiang University School of Medicine
Xiang Gao: Zhejiang University School of Medicine
Tongguan Tian: Zhejiang University School of Medicine
Zhaoyang Yu: Zhejiang University School of Medicine
Bo Gao: Zhejiang University School of Medicine
Aijia Wen: Zhejiang University School of Medicine
Linlin You: Chinese Academy of Sciences
Shenghai Chang: Zhejiang University School of Medicine
Xing Zhang: Zhejiang University School of Medicine
Yu Zhang: Chinese Academy of Sciences
Yu Feng: Zhejiang University School of Medicine

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: Abstract Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (QI and QII) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, QI forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well.

Date: 2019
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DOI: 10.1038/s41467-019-10958-8

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