Evidence map›Paper›PMID 36134607›Full record

ArticleProteins2023

Analysis of CheW-like domains provides insights into organization of prokaryotic chemotaxis systems.

Luke R Vass, Robert B Bourret, Clay A Foster

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Distinct roles of PilI and ChpC inApplied and environmental microbiology · 2026
    Article
  2. Microorganisms · 2025
    Review
  3. Proteomic Analysis of the Fish PathogenAnimals : an open access journal from MDPI · 2024
    Article
  4. Article
  5. Review
  6. 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 at 1 institution in 1 country.

Luke R VassDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, North Carolina, USA.
Robert B BourretDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, North Carolina, USA.ORCID 0000-0002-6666-9220
Clay A FosterDepartment of Microbiology & Immunology, University of North Carolina, Chapel Hill, North Carolina, USA.
University of North Carolina at Chapel Hill · US

Funding

Molecular Mechanisms of Signal Transduction by Two-Component Regulatory SystemsR01GM050860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BOURRET, ROBERT B. · 1994 to 2025
$7.9M
NIGMS NIH HHS R01 GM050860
6 · The paper itself

Abstract

The ability to control locomotion in a dynamic environment provides a competitive advantage for microorganisms, thus driving the evolution of sophisticated regulatory systems. In total, 19 known categories of chemotaxis systems control motility mediated by flagella or Type IV pili, plus other cellular functions. A key feature that distinguishes chemotaxis systems from generic two-component regulatory systems is separation of receptor and kinase functions into distinct proteins, linked by CheW scaffold proteins. This arrangement allows for formation of varied arrays with remarkable signaling properties. We recently analyzed sequences of CheW-like domains found in CheA kinases and CheW and CheV scaffold proteins. In total, 16 Architectures of CheA, CheW, and CheV proteins contain ~94% of all CheW-like domains and form six Classes with likely functional specializations. We surveyed chemotaxis system categories and proteins containing CheW-like domains in ~1900 prokaryotic species, the most comprehensive analysis to date, revealing new insights. Co-occurrence analyses suggested that many chemotaxis systems occur in non-random combinations within species, implying synergy or antagonism. Furthermore, many Architectures of proteins containing CheW-like domains occurred predominantly with specific categories of chemotaxis systems, suggesting specialized functional interactions. We propose Class 1 (~80%) and Class 6 (~20%) CheW proteins exhibit preferences for distinct chemoreceptor structures. Furthermore, rare (~1%) Class 2 CheW proteins frequently co-occurred with methyl-accepting coiled coil proteins, which contain both receptor and kinase functions and so do not require connection via a CheW scaffold but may benefit from arrays. Last, rare multidomain CheW proteins may interact with different receptors than single-domain CheW proteins.

Indexed as

ChemotaxisEscherichia coli ProteinsBacterial ProteinsCarrier ProteinsHistidine KinaseMethyl-Accepting Chemotaxis ProteinsSignal TransductionBacterial ProteinsCarrier ProteinsEscherichia coli ProteinsHistidine KinaseMethyl-Accepting Chemotaxis Proteinsbacterial chemotaxis systemsCheACheVCheWCheW-like domains

Identifiers

PMID36134607
PMCPMC9898116
OpenAlexW4296616750

What OpenQuestion holds

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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.