ArticleThe Journal of biological chemistry2013
X-ray crystal structure of Escherichia coli RNA polymerase σ70 holoenzyme.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.
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Who cites it
118 citing papers in PubMed, 189 citations in OpenAlex.
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- An Optimized Workflow for the Discovery of New Antimicrobial Compounds Targeting Bacterial RNA Polymerase Complex Formation.Antibiotics (Basel, Switzerland) · 2022Article
- Pseudomonas aeruginosa SutA wedges RNAP lobe domain open to facilitate promoter DNA unwinding.Nature communications · 2022Article
- Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase.Nature communications · 2022Article
- A non-native C-terminal extension of the β' subunit compromises RNA polymerase and Rho functions.Molecular microbiology · 2022Article
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- Role of bacterial RNA polymerase gate opening dynamics in DNA loading and antibiotics inhibition elucidated by quasi-Markov State Model.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Control of a programmed cell death pathway in Pseudomonas aeruginosa by an antiterminator.Nature communications · 2021Article
- Diverse and unified mechanisms of transcription initiation in bacteria.Nature reviews. Microbiology · 2021Review
- Structural basis of ribosomal RNA transcription regulation.Nature communications · 2021Article
- Watching the bacterial RNA polymerase transcription reaction by time-dependent soak-trigger-freeze X-ray crystallography.The Enzymes · 2021Review
- Genetic interaction mapping informs integrative structure determination of protein complexes.Science (New York, N.Y.) · 2020Article
58 more citing papers are in PubMed but not listed here.
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1 author at 1 institution in 1 country.
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Abstract
Escherichia coli RNA polymerase (RNAP) is the most studied bacterial RNAP and has been used as the model RNAP for screening and evaluating potential RNAP-targeting antibiotics. However, the x-ray crystal structure of E. coli RNAP has been limited to individual domains. Here, I report the x-ray structure of the E. coli RNAP σ(70) holoenzyme, which shows σ region 1.1 (σ1.1) and the α subunit C-terminal domain for the first time in the context of an intact RNAP. σ1.1 is positioned at the RNAP DNA-binding channel and completely blocks DNA entry to the RNAP active site. The structure reveals that σ1.1 contains a basic patch on its surface, which may play an important role in DNA interaction to facilitate open promoter complex formation. The α subunit C-terminal domain is positioned next to σ domain 4 with a fully stretched linker between the N- and C-terminal domains. E. coli RNAP crystals can be prepared from a convenient overexpression system, allowing further structural studies of bacterial RNAP mutants, including functionally deficient and antibiotic-resistant RNAPs.
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