Structures of Class I and Class II Transcription Complexes Reveal the Molecular Basis of RamA-Dependent Transcription Activation.

Structures of Class I and Class II Transcription Complexes Reveal the Molecular Basis of RamA-Dependent Transcription Activation.
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DOI:
10.1002/advs.202103669
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发表时间:
2022-03
期刊:
Advanced science (Weinheim, Baden-Wurttemberg, Germany)
影响因子:
--
通讯作者:
Wang M
Wang M
中科院分区:
其他
文献类型:
--
作者:
Hao M;Ye F;Jovanovic M;Kotta-Loizou I;Xu Q;Qin X;Buck M;Zhang X;Wang M

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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 70, together with activators, controls the majority of genes by recruiting RNA polymerase (RNAP) to the promoter regions. RNAP and σ 70 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 70 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. Transcription activator RamA is linked to multidrug resistance of Klebsiella pneumoniae. This study reveals the molecular basis for how RamA interacts with RNA polymerase (RNAP) and activates transcription that contributes to antibiotic resistance. Further, comparing with catabolite activator protein/thermophilic CAP homolog ( CAP/TAP) complexes reveals common and activator‐specific features in activator bindings and uncovers distinct roles of the two C‐terminal domains of RNAP.
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