Evidence map›Paper›PMID 20133868›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

T7 phage protein Gp2 inhibits the Escherichia coli RNA polymerase by antagonizing stable DNA strand separation near the transcription start site.

Beatriz Cámara, Minhao Liu, Jonathan Reynolds, Andrey Shadrin, Bing Liu, King Kwok, Peter Simpson, Robert Weinzierl, Konstantin Severinov, Ernesto Cota and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. RNA Management During T7 Infection.PHAGE (New Rochelle, N.Y.) · 2022
    Article
  8. 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
  9. The Phage-EncodedViruses · 2020
    Article
  10. NovelViruses · 2020
    Article
  11. Article
  12. Article
  13. T7 phage factor required for managing RpoS inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Mechanism of duplex DNA destabilization by RNA-guided Cas9 nuclease during target interrogation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Review
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

12 authors at 4 institutions in 3 countries.

Beatriz CámaraDepartment of Microbiology and Centre for Molecular Microbiology and Infection, Imperial College London, London SW7 2AZ, United Kingdom.
Minhao Liu
Jonathan Reynolds
Andrey Shadrin
Bing Liu
King Kwok
Peter Simpson
Robert Weinzierl
Konstantin Severinov
Ernesto Cota
Steve Matthews
Siva R Wigneshweraraj
Institute of Structural and Molecular Biology · GBG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RUImperial College London · GBRutgers, 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
Biotechnology and Biological Sciences Research Council BB/E023703Biotechnology and Biological Sciences Research Council BB/E023703/1Medical Research Council G0501703NIGMS NIH HHS GM59295NIGMS NIH HHS R01 GM059295
6 · The paper itself

Abstract

Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)--a multi-subunit enzyme responsible for gene transcription--by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex.

Indexed as

Bacteriophage T7Binding SitesDNA, BacterialDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsGenes, BacterialGenes, ViralModels, MolecularMultiprotein ComplexesMutationNuclear Magnetic Resonance, BiomolecularPromoter Regions, GeneticProtein ConformationRepressor ProteinsStatic ElectricityDNA, BacterialDNA-Directed RNA PolymerasesEscherichia coli Proteinsgene 2 product, bacteriophage T7Multiprotein ComplexesRepressor Proteins

Identifiers

PMID20133868
PMCPMC2836649
OpenAlexW2150237825

What OpenQuestion holds

Textmetadata
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.