Evidence map›Paper›PMID 24352426›Full record

ArticleGenes & development2013

Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein.

Aurelia Battesti, Joel R Hoskins, Song Tong, Paola Milanesio, Jessica M Mann, Andrea Kravats, Yodit M Tsegaye, Alexandre Bougdour, Sue Wickner, Susan Gottesman

Abstract read
In one paragraph

Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

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

10 authors.

Aurelia BattestiLaboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892, USA.
Joel R Hoskins
Song Tong
Paola Milanesio
Jessica M Mann
Andrea Kravats
Yodit M Tsegaye
Alexandre Bougdour
Sue Wickner
Susan Gottesman

Funding

Proteolysis and Regulation of Bacterial Cell Growth ControlZIABC011203 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GOTTESMAN, SUSAN · 2009 to 2025
$11.0M
Intramural NIH HHS
6 · The paper itself

Abstract

RpoS, an RNA polymerase σ factor, controls the response of Escherichia coli and related bacteria to multiple stress responses. During nonstress conditions, RpoS is rapidly degraded by ClpXP, mediated by the adaptor protein RssB, a member of the response regulator family. In response to stress, RpoS degradation ceases. Small anti-adaptor proteins--IraP, IraM, and IraD, each made under a different stress condition--block RpoS degradation. RssB mutants resistant to either IraP or IraM were isolated and analyzed in vivo and in vitro. Each of the anti-adaptors is unique in its interaction with RssB and sensitivity to RssB mutants. One class of mutants defined an RssB N-terminal region close to the phosphorylation site and critical for interaction with IraP but unnecessary for IraM and IraD function. A second class, in the RssB C-terminal PP2C-like domain, led to activation of RssB function. These mutants allowed the response regulator to act in the absence of phosphorylation but did not abolish interaction with anti-adaptors. This class of mutants is broadly resistant to the anti-adaptors and bears similarity to constitutively activated mutants found in a very different PP2C protein. The mutants provide insight into how the anti-adaptors perturb RssB response regulator function and activation.

Indexed as

Gene Expression Regulation, BacterialBacterial ProteinsDNA-Binding ProteinsEscherichia coli K12Escherichia coli ProteinsMutationPhosphorylationProtein Structure, TertiaryTranscription FactorsBacterial ProteinsDNA-Binding ProteinsEscherichia coli ProteinsIraM protein, E coliIraP protein, E colirssB protein, E coliTranscription FactorsClpXIraPresponse regulatorRpoSRsbP

Identifiers

PMID24352426
PMCPMC3877760

What OpenQuestion holds

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LicenceCC BY-NC
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.