Evidence map›Paper›PMID 15489452›Full record

ArticleJournal of bacteriology2004

RpoS proteolysis is regulated by a mechanism that does not require the SprE (RssB) response regulator phosphorylation site.

Celeste N Peterson, Natividad Ruiz, Thomas J Silhavy

Abstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. RpoS and the bacterial general stress response.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  3. Article
  4. Structure of phosphorylated-like RssB, the adaptor delivering σThe Journal of biological chemistry · 2023
    Article
  5. A negative feedback loop is critical for recovery of RpoS after stress inbioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Control of theEcoSal Plus · 2019
    Review
  11. Review
  12. Article
  13. ClpP Protease, a Promising Antimicrobial Target.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. 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

3 authors.

Celeste N PetersonDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Natividad Ruiz
Thomas J Silhavy

Funding

Regulation of Stationary Phase in Escherichia coliR01GM065216 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 2003 to 2014
$3.5M
NIGMS NIH HHS GM 65216NIGMS NIH HHS R01 GM065216
6 · The paper itself

Abstract

In Escherichia coli the response regulator SprE (RssB) facilitates degradation of the sigma factor RpoS by delivering it to the ClpXP protease. This process is regulated: RpoS is degraded in logarithmic phase but becomes stable upon carbon starvation, resulting in its accumulation. Because SprE contains a CheY domain with a conserved phosphorylation site (D58), the prevailing model posits that this control is mediated by phosphorylation. To test this model, we mutated the conserved response regulator phosphorylation site (D58A) of the chromosomal allele of sprE and monitored RpoS levels in response to carbon starvation. Though phosphorylation contributed to the SprE basal activity, we found that RpoS proteolysis was still regulated upon carbon starvation. Furthermore, our results indicate that phosphorylation of wild-type SprE occurs by a mechanism that is independent of acetyl phosphate.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsCulture MediaDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGlucoseOrganophosphatesPhosphorylationSigma FactorTranscription Factorsacetyl phosphateBacterial ProteinsCulture MediaDNA-Binding ProteinsEscherichia coli ProteinsGlucoseOrganophosphatesrssB protein, E coliSigma Factorsigma factor KatF protein, BacteriaTranscription Factors

Identifiers

PMID15489452
PMCPMC523208

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.