Evidence map›Paper›PMID 16291649›Full record

ArticleGenes & development2005

A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli.

Franziska Mika, Regine Hengge

Abstract read
In one paragraph

Article in Genes & development, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing 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

88 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Crosstalk involving two-component systems inJournal of bacteriology · 2024
    Review
  7. Article
  8. RpoS and the bacterial general stress response.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  9. Article
  10. Review
  11. Structure of phosphorylated-like RssB, the adaptor delivering σThe Journal of biological chemistry · 2023
    Article
  12. A negative feedback loop is critical for recovery of RpoS after stress inbioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. The ArcAB Two-Component System: Function in Metabolism, Redox Control, and Infection.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  17. Article
  18. Review
  19. Review
  20. The role of l-arabinose metabolism forMicrobiology (Reading, England) · 2021
    Article

28 more citing papers are in PubMed but not listed here.

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.

Franziska MikaInstitut für Biologie-Mikrobiologie, Freie Universität Berlin, Germany.
Regine Hengge

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The general stress sigma factor sigma(S) (RpoS) in Escherichia coli is controlled at the levels of transcription, translation, and proteolysis. Here we demonstrate that the phosphorylated response regulator ArcA is a direct repressor of rpoS transcription that binds to two sites flanking the major rpoS promoter, with the upstream site overlapping an activating cAMP-CRP-binding site. The histidine sensor kinase ArcB not only phosphorylates ArcA, but also the sigma(S) proteolytic targeting factor RssB, and thereby stimulates sigma(S) proteolysis. Thus, ArcB/ArcA/RssB constitute a branched "three-component system", which coordinates rpoS transcription and sigma(S) proteolysis and thereby maintains low sigma(S) levels in rapidly growing cells. We suggest that the redox state of the quinones, which controls autophosphorylation of ArcB, not only monitors oxygen but also energy supply, and we show that the ArcB/ArcA/RssB system is involved in sigma(S) induction during entry into starvation conditions. Moreover, this induction is enhanced by a positive feedback that involves sigma(S)-dependent induction of ArcA, which further reduces sigma(S) proteolysis, probably by competing with RssB for residual phosphorylation by ArcB.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialHydrolysisMembrane ProteinsMutationPhosphorylationPhosphotransferasesProtein KinasesRepressor ProteinsSigma FactorTranscription FactorsTranscription, GeneticarcA protein, E coliarcB protein, E coliBacterial Outer Membrane ProteinsBacterial ProteinsDNA-Binding ProteinsEscherichia coli ProteinsMembrane ProteinsPhosphotransferasesProtein KinasesRepressor ProteinsrssB protein, E coliSigma Factorsigma factor KatF protein, BacteriaTranscription Factors

Identifiers

PMID16291649
PMCPMC1283968

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.