Evidence map›Paper›PMID 22819324›Full record

ArticleMolecular cell2012

Structural and mechanistic basis for the inhibition of Escherichia coli RNA polymerase by T7 Gp2.

Ellen James, Minhao Liu, Carol Sheppard, Vladimir Mekler, Beatriz Cámara, Bing Liu, Pete Simpson, Ernesto Cota, Konstantin Severinov, Steve Matthews and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 47 citations in OpenAlex.

  1. RNA Management During T7 Infection.PHAGE (New Rochelle, N.Y.) · 2022
    Article
  2. Article
  3. Bacteriophage protein Gp46 is a cross-species inhibitor of nucleoid-associated HU proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. The Phage-EncodedViruses · 2020
    Article
  8. T7 phage factor required for managing RpoS inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Article
  11. Article
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  15. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 4 countries.

Ellen JamesMRC Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, UK.
Minhao Liu
Carol Sheppard
Vladimir Mekler
Beatriz Cámara
Bing Liu
Pete Simpson
Ernesto Cota
Konstantin Severinov
Steve Matthews
Sivaramesh Wigneshweraraj
Imperial College London · GBFederico Santa María Technical University · CLInstitute of Gene Biology · RURutgers, The State University of New Jersey · US

Funding

Phage-induced modifications of RNA polymeraseR01GM059295 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI SEVERINOV, KONSTANTIN V · 1999 to 2013
$4.5M
Structure-based mutational analysis of RNA polymeraseR01GM064530 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI SEVERINOV, KONSTANTIN V · 2002 to 2010
$2.7M
Biotechnology and Biological Sciences Research Council BB/E023703Biotechnology and Biological Sciences Research Council BB/E023703/1NIGMS NIH HHS GM59295NIGMS NIH HHS GM64530NIGMS NIH HHS R01 GM059295NIGMS NIH HHS R01 GM064530Wellcome Trust
6 · The paper itself

Abstract

The T7 phage-encoded small protein Gp2 is a non-DNA-binding transcription factor that interacts with the jaw domain of the Escherichia coli (Ec) RNA polymerase (RNAp) β' subunit and inhibits transcriptionally proficient promoter-complex (RPo) formation. Here, we describe the high-resolution solution structure of the Gp2-Ec β' jaw domain complex and show that Gp2 and DNA compete for binding to the β' jaw domain. We reveal that efficient inhibition of RPo formation by Gp2 requires the amino-terminal σ(70) domain region 1.1 (R1.1), and that Gp2 antagonizes the obligatory movement of R1.1 during RPo formation. We demonstrate that Gp2 inhibits RPo formation not just by steric occlusion of the RNAp-DNA interaction but also through long-range antagonistic effects on RNAp-promoter interactions around the RNAp active center that likely occur due to repositioning of R1.1 by Gp2. The inhibition of Ec RNAp by Gp2 thus defines a previously uncharacterized mechanism by which bacterial transcription is regulated by a viral factor.

Indexed as

DNA, BacterialDNA-Directed RNA PolymerasesEscherichia coliModels, MolecularPromoter Regions, GeneticProtein ConformationRepressor ProteinsTranscriptional ActivationTranscription, GeneticDNA, BacterialDNA-Directed RNA Polymerasesgene 2 product, bacteriophage T7Repressor Proteins

Identifiers

PMID22819324
PMCPMC3778932
OpenAlexW1967725326

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.