Pseudomonas aeruginosa SutA wedges RNAP lobe domain open to facilitate promoter DNA unwinding

Dingwei He, Linlin You, Xiaoxian Wu, Jing Shi, Aijia Wen, Zhi Yan, Wenhui Mu, Chengli Fang, Yu Feng () and Yu Zhang ()
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Dingwei He: Chinese Academy of Sciences
Linlin You: Chinese Academy of Sciences
Xiaoxian Wu: Chinese Academy of Sciences
Jing Shi: Nanjing University of Chinese Medicine
Aijia Wen: Zhejiang University School of Medicine
Zhi Yan: Chinese Academy of Sciences
Wenhui Mu: Chinese Academy of Sciences
Chengli Fang: Chinese Academy of Sciences
Yu Feng: Zhejiang University School of Medicine
Yu Zhang: Chinese Academy of Sciences

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract Pseudomonas aeruginosa (Pae) SutA adapts bacteria to hypoxia and nutrition-limited environment during chronic infection by increasing transcription activity of an RNA polymerase (RNAP) holoenzyme comprising the stress-responsive σ factor σS (RNAP-σS). SutA shows no homology to previously characterized RNAP-binding proteins. The structure and mode of action of SutA remain unclear. Here we determined cryo-EM structures of Pae RNAP-σS holoenzyme, Pae RNAP-σS holoenzyme complexed with SutA, and Pae RNAP-σS transcription initiation complex comprising SutA. The structures show SutA pinches RNAP-β protrusion and facilitates promoter unwinding by wedging RNAP-β lobe open. Our results demonstrate that SutA clears an energetic barrier to facilitate promoter unwinding of RNAP-σS holoenzyme.

Date: 2022
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DOI: 10.1038/s41467-022-31871-7

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