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

被引：0
作者：
Chengli Fang
Linyu Li
Yihan Zhao
Xiaoxian Wu
Steven J. Philips
Linlin You
Mingkang Zhong
Xiaojin Shi
Thomas V. O’Halloran
Qunyi Li
Yu Zhang
机构：
[1] Chinese Academy of Sciences,Key Laboratory of Synthetic Biology, CAS Center for Excellence in Molecular Plant Sciences
[2] University of Chinese Academy of Sciences,Clinical Pharmacy Laboratory, Huashan Hospital
[3] Fudan University,Key Laboratory of Plant Stress Biology, State Key Laboratory of Cotton Biology, School of Life Sciences
[4] Henan University,Department of Chemistry
[5] Northwestern University,Department of Molecular Biosciences
[6] Northwestern University,The Chemistry of Life Processes Institute
[7] Northwestern University,undefined
来源：
Nature Communications | / 11卷
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摘要：
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.
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