ReviewArchaea (Vancouver, B.C.)2011
The Bridge Helix of RNA polymerase acts as a central nanomechanical switchboard for coordinating catalysis and substrate movement.
Review in Archaea (Vancouver, B.C.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed.
- Structure of plant RNA-DEPENDENT RNA POLYMERASE 2, an enzyme involved in small interfering RNA production.The Plant cell · 2022Article
- Structure and RNA template requirements ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Transcribing Genes the Hard Way:Frontiers in molecular biosciences · 2021Article
- Article
- Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases.PLoS biology · 2019Article
- Hinge action versus grip in translocation by RNA polymerase.Transcription · 2018Article
- Insights into RNA polymerase catalysis and adaptive evolution gained from mutational analysis of a locus conferring rifampicin resistance.Nucleic acids research · 2017Article
- Molecular Structures of Transcribing RNA Polymerase I.Molecular cell · 2016Article
- Computational simulation strategies for analysis of multisubunit RNA polymerases.Chemical reviews · 2013Review
- Article
- The RNA polymerase bridge helix YFI motif in catalysis, fidelity and translocation.Biochimica et biophysica acta · 2013Article
- Basic mechanism of transcription by RNA polymerase II.Biochimica et biophysica acta · 2013Review
- Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
The availability of in vitro assembly systems to produce recombinant archaeal RNA polymerases (RNAPs) offers one of the most powerful experimental tools for investigating the still relatively poorly understood molecular mechanisms underlying RNAP function. Over the last few years, we pioneered new robot-based high-throughput mutagenesis approaches to study structure/function relationships within various domains surrounding the catalytic center. The Bridge Helix domain, which appears in numerous X-ray structures as a 35-amino-acid-long alpha helix, coordinates the concerted movement of several other domains during catalysis through kinking of two discrete molecular hinges. Mutations affecting these kinking mechanisms have a direct effect on the specific catalytic activity of RNAP and can in some instances more than double it. Molecular dynamics simulations have established themselves as exceptionally useful for providing additional insights and detailed models to explain the underlying structural motions.
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Registered trials
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