The bacterial multidrug resistance regulator BmrR distorts promoter DNA to activate transcription
| Autor: | Yihan Zhao, Thomas V. O'Halloran, Qunyi Li, Chengli Fang, Steven J. Philips, Xiaojin Shi, Yu Zhang, Linyu Li, Xiaoxian Wu, Linlin You, Mingkang Zhong |
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| Rok vydání: | 2020 |
| Předmět: |
Transcriptional Activation
0301 basic medicine Science genetic processes General Physics and Astronomy Biochemistry Article General Biochemistry Genetics and Molecular Biology Bacterial genetics 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Bacterial Proteins Cryoelectron microscopy Transcription (biology) Bacterial transcription Drug Resistance Multiple Bacterial RNA polymerase Promoter Regions Genetic Transcription factor chemistry.chemical_classification Regulation of gene expression Multidisciplinary Promoter DNA-Directed RNA Polymerases Gene Expression Regulation Bacterial General Chemistry Cell biology 030104 developmental biology Enzyme chemistry Trans-Activators 030217 neurology & neurosurgery Bacillus subtilis |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. BmrR is a member of the bacterial MerR transcription factor family that regulates the expression of the bacterial efflux pump Bmr. Here, the authors present the cryo-EM structure of a B. subtilis transcription activation complex (TAC) containing the RNA Polymerase (RNAP) core enzyme, σA, promoter DNA and ligand-bound BmrR, which reveals that in contrast to most other transcription factors BmrR does not directly interact with RNAP and instead activates transcription by modulating the shape of the core promoter. |
| Databáze: | OpenAIRE |
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