Biotechnology and Biological Sciences Research Council (BBSRC)
BB/N007816/1
United Kingdom
Medical Research Council (MRC, United Kingdom)
MR/P007503/1
United Kingdom
National Science Foundation (NSF, China)
81991531
China
Citation
Journal: Adv Sci (Weinh) / Year: 2022 Title: Structures of Class I and Class II Transcription Complexes Reveal the Molecular Basis of RamA-Dependent Transcription Activation. Authors: Min Hao / Fuzhou Ye / Milija Jovanovic / Ioly Kotta-Loizou / Qingqing Xu / Xiaohua Qin / Martin Buck / Xiaodong Zhang / Minggui Wang / 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 ...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, σ , together with activators, controls the majority of genes by recruiting RNA polymerase (RNAP) to the promoter regions. RNAP and σ 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-σ 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.
History
Deposition
Dec 23, 2020
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Header (metadata) release
Dec 1, 2021
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Map release
Dec 1, 2021
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Update
Feb 16, 2022
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Current status
Feb 16, 2022
Processing site: PDBe / Status: Released
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