Evidence map›Paper›PMID 18826409›Full record

ArticleMolecular microbiology2008

Rsd family proteins make simultaneous interactions with regions 2 and 4 of the primary sigma factor.

Andy H Yuan, Brian D Gregory, Josh S Sharp, Katherine D McCleary, Simon L Dove, Ann Hochschild

Abstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. RpoS and the bacterial general stress response.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  2. Article
  3. Article
  4. Review
  5. Linking glucose metabolism to the stringent response through the PTS.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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
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

6 authors.

Andy H YuanDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.
Brian D Gregory
Josh S Sharp
Katherine D McCleary
Simon L Dove
Ann Hochschild

Funding

INFECTIOUS DISEASE AND BASIC MICROBIOLOGICAL MECHANISMST32AI007061 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI Marcia B Goldberg · 1985 to 2026
$12.1M
PROTEIN/PROTEIN INTERACTIONS IN PROKARYOTIC GENE CONTROLR01GM044025 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HOCHSCHILD, ANN · 1990 to 2015
$8.1M
Transcription Regulation in Pseudomonas aeruginosaR01AI057754 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI DOVE, SIMON L · 2006 to 2010
$1.8M
Phase-variable gene expression in Pseudomonas aeruginosaR01AI069007 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI DOVE, SIMON L · 2006 to 2010
$1.8M
NIAID NIH HHS AI057754NIAID NIH HHS AI069007NIAID NIH HHS R01 AI057754NIAID NIH HHS R01 AI069007NIAID NIH HHS T32 AI007061NIGMS NIH HHS GM44025NIGMS NIH HHS R01 GM044025
6 · The paper itself

Abstract

Bacterial anti-sigma factors typically regulate sigma factor function by restricting the access of their cognate sigma factors to the RNA polymerase (RNAP) core enzyme. The Escherichia coli Rsd protein forms a complex with the primary sigma factor, sigma(70), inhibits sigma(70)-dependent transcription in vitro, and has been proposed to function as a sigma(70)-specific anti-sigma factor, thereby facilitating the utilization of alternative sigma factors. In prior work, Rsd has been shown to interact with conserved region 4 of sigma(70), but it is not known whether this interaction suffices to account for the regulatory functions of Rsd. Here we show that Rsd and the Rsd orthologue AlgQ, a global regulator of gene expression in Pseudomonas aeruginosa, interact with conserved region 2 of sigma(70). We show further that Rsd and AlgQ can interact simultaneously with regions 2 and 4 of sigma(70). Our findings establish that the abilities of Rsd and AlgQ to interact with sigma(70) region 2 are important determinants of their in vitro and in vivo activities.

Indexed as

Amino Acid SubstitutionBacterial ProteinsDNA, BacterialDNA-Directed RNA PolymerasesGene DeletionGene Expression Regulation, BacterialGenes, BacterialMutationPlasmidsProtein BindingPseudomonas aeruginosaPyocyanineRepressor ProteinsSigma FactorTrans-ActivatorsTranscription, GeneticAlgQ protein, Pseudomonas aeruginosaBacterial ProteinsDNA, BacterialDNA-Directed RNA PolymerasesPyocyanineRepressor ProteinsRNA polymerase sigma 70Sigma FactorTrans-Activators

Identifiers

PMID18826409
PMCPMC2581641

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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.