Evidence map›Paper›PMID 35648808›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Co-component signal transduction systems: Fast-evolving virulence regulation cassettes discovered in enteric bacteria.

Lisa N Kinch, Qian Cong, Jananee Jaishankar, Kim Orth

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Effects of Bile on PathogenicBiomolecules · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. eLife · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Lisa N KinchDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Qian CongEugene McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center, Dallas, TX 75390.ORCID 0000-0002-8909-0414
Jananee JaishankarDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Kim OrthDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390.ORCID 0000-0002-0678-7620
The University of Texas Southwestern Medical Center · USSouthwestern Medical Center · US

Funding

Biochemistry, biology and diversity of Fic domainsR35GM134945 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2020 to 2024
$1.8M
Proteostasis, AMPylation and the Unfolded Protein repsonse (UPR)R01GM115188 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ORTH, KIM · 2015 to 2018
$1.2M
NIGMS NIH HHS R01 GM115188NIGMS NIH HHS R35 GM134945
6 · The paper itself

Abstract

Bacterial signal transduction systems sense changes in the environment and transmit these signals to control cellular responses. The simplest one-component signal transduction systems include an input sensor domain and an output response domain encoded in a single protein chain. Alternatively, two-component signal transduction systems transmit signals by phosphorelay between input and output domains from separate proteins. The membrane-tethered periplasmic bile acid sensor that activates the Vibrio parahaemolyticus type III secretion system adopts an obligate heterodimer of two proteins encoded by partially overlapping VtrA and VtrC genes. This co-component signal transduction system binds bile acid using a lipocalin-like domain in VtrC and transmits the signal through the membrane to a cytoplasmic DNA-binding transcription factor in VtrA. Using the domain and operon organization of VtrA/VtrC, we identify a fast-evolving superfamily of co-component systems in enteric bacteria. Accurate machine learning–based fold predictions for the candidate co-components support their homology in the twilight zone of rapidly evolving sequences and provide mechanistic hypotheses about previously unrecognized lipid-sensing functions.

Indexed as

Bacterial ProteinsGene Expression Regulation, BacterialGenomic IslandsMembrane ProteinsType III Secretion SystemsVibrio parahaemolyticusBile Acids and SaltsDNA-Binding ProteinsProtein MultimerizationSignal TransductionTranscription FactorsVirulenceBacterial ProteinsBile Acids and SaltsDNA-Binding ProteinsMembrane ProteinstoxR protein, bacteriaTranscription FactorsType III Secretion Systemsco-component signal transduction systementeric bacteriaprotein sequence evolutionprotein structure predictionvirulence transcription regulation

Identifiers

PMID35648808
PMCPMC9214523
OpenAlexW4281941988

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.