Evidence map›Paper›PMID 11591686›Full record

ArticleJournal of bacteriology2001

Bacterial two-hybrid analysis of interactions between region 4 of the sigma(70) subunit of RNA polymerase and the transcriptional regulators Rsd from Escherichia coli and AlgQ from Pseudomonas aeruginosa.

S L Dove, A Hochschild

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  11. Review
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  13. A two-subunit bacterial sigma-factor activates transcription in Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Article
  16. The bacteriophage T4 AsiA protein contacts the beta-flap domain of RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  17. Article
  18. Article
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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

2 authors at 1 institution in 1 country.

S L DoveDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
A Hochschild
Harvard University · US

Funding

PROTEIN/PROTEIN INTERACTIONS IN PROKARYOTIC GENE CONTROLR01GM044025 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOCHSCHILD, ANN · 1990 to 2015
$8.1M
NIGMS NIH HHS GM44025NIGMS NIH HHS R01 GM044025
6 · The paper itself

Abstract

A number of transcriptional regulators mediate their effects through direct contact with the sigma(70) subunit of Escherichia coli RNA polymerase (RNAP). In particular, several regulators have been shown to contact a C-terminal portion of sigma(70) that harbors conserved region 4. This region of sigma contains a putative helix-turn-helix DNA-binding motif that contacts the -35 element of sigma(70)-dependent promoters directly. Here we report the use of a recently developed bacterial two-hybrid system to study the interaction between the putative anti-sigma factor Rsd and the sigma(70) subunit of E. coli RNAP. Using this system, we found that Rsd can interact with an 86-amino-acid C-terminal fragment of sigma(70) and also that amino acid substitution R596H, within region 4 of sigma(70), weakens this interaction. We demonstrated the specificity of this effect by showing that substitution R596H does not weaken the interaction between sigma and two other regulators shown previously to contact region 4 of sigma(70). We also demonstrated that AlgQ, a homolog of Rsd that positively regulates virulence gene expression in Pseudomonas aeruginosa, can contact the C-terminal region of the sigma(70) subunit of RNAP from this organism. We found that amino acid substitution R600H in sigma(70) from P. aeruginosa, corresponding to the R596H substitution in E. coli sigma(70), specifically weakens the interaction between AlgQ and sigma(70). Taken together, our findings suggest that Rsd and AlgQ contact similar surfaces of RNAP present in region 4 of sigma(70) and probably regulate gene expression through this contact.

Indexed as

Escherichia coli ProteinsGene Expression Regulation, BacterialAmino Acid SubstitutionBacterial ProteinsBacteriophage lambdaConserved SequenceDNA-Directed RNA PolymerasesEscherichia coliModels, GeneticPromoter Regions, GeneticProtein KinasesPseudomonas aeruginosaRecombinant Fusion ProteinsRepressor ProteinsSigma FactorTrans-ActivatorsAlgQ protein, Pseudomonas aeruginosaAsiA protein, Enterobacteria phage T4Bacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsProtein KinasesRecombinant Fusion ProteinsRepressor ProteinsRNA polymerase sigma 70Rsd protein, E coliSigma FactorTrans-ActivatorsTranscription FactorsViral Proteins

Identifiers

PMID11591686
PMCPMC100137
OpenAlexW2165730924

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.