Evidence map›Paper›PMID 22194454›Full record

ArticleJournal of bacteriology2012

Sinorhizobium meliloti CheA complexed with CheS exhibits enhanced binding to CheY1, resulting in accelerated CheY1 dephosphorylation.

Gaurav Dogra, Frauke G Purschke, Verena Wagner, Martin Haslbeck, Thomas Kriehuber, Jonathan G Hughes, Maxwell L Van Tassell, Crystal Gilbert, Melanie Niemeyer, W Keith Ray and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Microorganisms · 2025
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  5. The Only Chemoreceptor Encoded byMicroorganisms · 2021
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  6. Diversity of bacterial chemosensory systems.Current opinion in microbiology · 2021
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  7. The Divergent Key Residues of TwoMicroorganisms · 2021
    Article
  8. Review
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  11. Review
  12. An Updated Perspective onFrontiers in microbiology · 2020
    Article
  13. Article
  14. AApplied and environmental microbiology · 2018
    Article
  15. Review
  16. Article
  17. Article
  18. 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

12 authors at 3 institutions in 2 countries.

Gaurav DograVirginia Tech, Biological Sciences, Blacksburg, Virginia, USA.
Frauke G Purschke
Verena Wagner
Martin Haslbeck
Thomas Kriehuber
Jonathan G Hughes
Maxwell L Van Tassell
Crystal Gilbert
Melanie Niemeyer
W Keith Ray
Richard F Helm
Birgit E Scharf
Virginia Tech · USUniversity of Regensburg · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Retrophosphorylation of the histidine kinase CheA in the chemosensory transduction chain is a widespread mechanism for efficient dephosphorylation of the activated response regulator. First discovered in Sinorhizobium meliloti, the main response regulator CheY2-P shuttles its phosphoryl group back to CheA, while a second response regulator, CheY1, serves as a sink for surplus phosphoryl groups from CheA-P. We have identified a new component in this phospho-relay system, a small 97-amino-acid protein named CheS. CheS has no counterpart in enteric bacteria but revealed distinct similarities to proteins of unknown function in other members of the α subgroup of proteobacteria. Deletion of cheS causes a phenotype similar to that of a cheY1 deletion strain. Fluorescence microscopy revealed that CheS is part of the polar chemosensory cluster and that its cellular localization is dependent on the presence of CheA. In vitro binding, as well as coexpression and copurification studies, gave evidence of CheA/CheS complex formation. Using limited proteolysis coupled with mass spectrometric analyses, we defined CheA(163-256) to be the CheS binding domain, which overlaps with the N-terminal part of the CheY2 binding domain (CheA(174-316)). Phosphotransfer experiments using isolated CheA-P showed that dephosphorylation of CheY1-P but not CheY2-P is increased in the presence of CheS. As determined by surface plasmon resonance spectroscopy, CheY1 binds ∼100-fold more strongly to CheA/CheS than to CheA. We propose that CheS facilitates signal termination by enhancing the interaction of CheY1 and CheA, thereby promoting CheY1-P dephosphorylation, which results in a more efficient drainage of the phosphate sink.

Indexed as

Gene Expression Regulation, BacterialProtein Interaction MappingProtein Processing, Post-TranslationalSignal TransductionAmino Acid SequenceBacterial ProteinsCell MembraneCytosolGene DeletionMass SpectrometryMicroscopy, FluorescenceMolecular Sequence DataPhosphorylationProtein Interaction Domains and MotifsProteolysisSequence Homology, Amino AcidBacterial Proteins

Identifiers

PMID22194454
PMCPMC3294773
OpenAlexW2140559567

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.