Evidence map›Paper›PMID 26635367›Full record

ArticleThe Journal of biological chemistry2016

Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli.

Derk Pannen, Maria Fabisch, Lisa Gausling, Karin Schnetz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. A frameshift ineLife · 2023
    Article
  10. Article
  11. Article
  12. Novel Virulence Factors DecipheringInternational journal of molecular sciences · 2022
    Article
  13. Article
  14. Article
  15. Regulation ofMicrobiology (Reading, England) · 2022
    Article
  16. Impact of Sub-MIC Eugenol onFrontiers in veterinary science · 2022
    Article
  17. Regulation of gene expression by non-phosphorylated response regulators.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    Review
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Derk PannenFrom the Institute for Genetics, University of Cologne, Zülpicher Strasse 47a, 50674 Cologne, Germany.
Maria FabischFrom the Institute for Genetics, University of Cologne, Zülpicher Strasse 47a, 50674 Cologne, Germany.
Lisa GauslingFrom the Institute for Genetics, University of Cologne, Zülpicher Strasse 47a, 50674 Cologne, Germany.
Karin SchnetzFrom the Institute for Genetics, University of Cologne, Zülpicher Strasse 47a, 50674 Cologne, Germany schnetz@uni-koeln.de.
University of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rcs phosphorelay is a two-component signal transduction system that is induced by cell envelope stress. RcsB, the response regulator of this signaling system, is a pleiotropic transcription regulator, which is involved in the control of various stress responses, cell division, motility, and biofilm formation. RcsB regulates transcription either as a homodimer or together with auxiliary regulators, such as RcsA, BglJ, and GadE in Escherichia coli. In this study, we show that RcsB in addition forms heterodimers with MatA (also known as EcpR) and with DctR. Our data suggest that the MatA-dependent transcription regulation is mediated by the MatA-RcsB heterodimer and is independent of RcsB phosphorylation. Furthermore, we analyzed the relevance of amino acid residues of the active quintet of conserved residues, and of surface-exposed residues for activity of RcsB. The data suggest that the activity of the phosphorylation-dependent dimers, such as RcsA-RcsB and RcsB-RcsB, is affected by mutation of residues in the vicinity of the phosphorylation site, suggesting that a phosphorylation-induced structural change modulates their activity. In contrast, the phosphorylation-independent heterodimers BglJ-RcsB and MatA-RcsB are affected by only very few mutations. Heterodimerization of RcsB with various auxiliary regulators and their differential dependence on phosphorylation add an additional level of control to the Rcs system that is operating at the output level.

Indexed as

Gene Expression Regulation, Bacterialbeta-GalactosidaseCell MembraneEscherichia coliEscherichia coli ProteinsGenome, BacterialLipoproteinsMolecular ConformationMutationOligonucleotide Array Sequence AnalysisOligonucleotidesPhosphorylationPlasmidsProtein MultimerizationRNASignal Transductionbeta-GalactosidaseBglJ protein, E coliDctR protein, E coliEcpR protein, E coliEscherichia coli ProteinsLipoproteinsOligonucleotidesRcsA protein, E coliRcsB protein, E coliRNATrans-ActivatorsTranscription Factorsbacterial signal transductionDNA binding proteinprotein phosphorylationprotein-protein interactiontranscription coregulator

Identifiers

PMID26635367
PMCPMC4732218
OpenAlexW2182982294

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.