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Structures of class I and class II transcription complexes reveal the molecular basis of RamA-dependent transcription activation

DOI: 10.1002/advs.202103669 DOI Help

Authors: Min Hao (Huashan Hospital, Fudan University; National Health Commission of the People’s Republic of China; Imperial College London) , Fuzhou Ye (Imperial College London) , Milija Jovanovic (Imperial College London) , Ioly Kotta‐loizou (Imperial College London) , Qingqing Xu (Huashan Hospital, Fudan University; National Health Commission of the People’s Republic of China) , Xiaohua Qin (Huashan Hospital, Fudan University; National Health Commission of the People’s Republic of China; Imperial College London) , Martin Buck (Imperial College London) , Xiaodong Zhang (Imperial College London) , Minggui Wang (Huashan Hospital, Fudan University; National Health Commission of the People’s Republic of China)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Advanced Science , VOL 141

State: Published (Approved)
Published: November 2021
Diamond Proposal Number(s): 19865

Open Access Open Access

Abstract: Transcription activator RamA is linked to multidrug resistance of Klebsiella pneumoniae through controlling genes that encode efflux pumps (acrA) and porin-regulating antisense RNA (micF). In bacteria, σ70, together with activators, controls the majority of genes by recruiting RNA polymerase (RNAP) to the promoter regions. RNAP and σ70 form a holoenzyme that recognizes -35 and -10 promoter DNA consensus sites. Many activators bind upstream from the holoenzyme and can be broadly divided into two classes. RamA acts as a class I activator on acrA and class II activator on micF, respectively. The authors present biochemical and structural data on RamA in complex with RNAP-σ70 at the two promoters and the data reveal the molecular basis for how RamA assembles and interacts with core RNAP and activates transcription that contributes to antibiotic resistance. Further, comparing with CAP/TAP complexes reveals common and activator-specific features in activator binding and uncovers distinct roles of the two C-terminal domains of RNAP α subunit.

Journal Keywords: antibiotic resistance; class I and class II activators; cryoEM structures; RamA; RNAP-𝜎70

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Chemistry, Medicine

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond , Krios IV-Titan Krios IV at Diamond

Added On: 11/11/2021 10:24

Documents:
advs.202103669.pdf

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Antibiotic Resistance Infectious Diseases Pathogens Structural biology Chemistry Biochemistry

Technical Tags:

Microscopy Electron Microscopy (EM) Cryo Electron Microscopy (Cryo EM)