The bacterial multidrug resistance regulator BmrR distorts promoter DNA to activate transcription

Chengli Fang, Linyu Li, Yihan Zhao, Xiaoxian Wu, Steven J. Philips, Linlin You, Mingkang Zhong, Xiaojin Shi, Thomas V. O’Halloran, Qunyi Li () and Yu Zhang ()
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Chengli Fang: Chinese Academy of Sciences
Linyu Li: Fudan University
Yihan Zhao: Henan University
Xiaoxian Wu: Chinese Academy of Sciences
Steven J. Philips: Northwestern University
Linlin You: Chinese Academy of Sciences
Mingkang Zhong: Fudan University
Xiaojin Shi: Fudan University
Thomas V. O’Halloran: Northwestern University
Qunyi Li: Fudan University
Yu Zhang: Chinese Academy of Sciences

Nature Communications, 2020, vol. 11, issue 1, 1-9

Abstract: Abstract The MerR-family proteins represent a unique family of bacteria transcription factors (TFs), which activate transcription in a manner distinct from canonical ones. Here, we report a cryo-EM structure of a B. subtilis transcription activation complex comprising B. subtilis six-subunit (2αββ‘ωε) RNA Polymerase (RNAP) core enzyme, σA, a promoter DNA, and the ligand-bound B. subtilis BmrR, a prototype of MerR-family TFs. The structure reveals that RNAP and BmrR recognize the upstream promoter DNA from opposite faces and induce four significant kinks from the −35 element to the −10 element of the promoter DNA in a cooperative manner, which restores otherwise inactive promoter activity by shortening the length of promoter non-optimal −35/−10 spacer. Our structure supports a DNA-distortion and RNAP-non-contact paradigm of transcriptional activation by MerR TFs.

Date: 2020
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DOI: 10.1038/s41467-020-20134-y

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