Evidence map›Paper›PMID 9560203›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.

R Ramakrishnan, M Schuster, R B Bourret

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-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

28 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Contribution of NmSystems · 2021
    Article
  6. TheMicrobiology (Reading, England) · 2021
    Article
  7. Review
  8. Expression ofMicroorganisms · 2020
    Article
  9. Article
  10. Structure and function of the archaeal response regulator CheY.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Review
  12. Review
  13. Glycolysis for Microbiome Generation.Microbiology spectrum · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The acetate switch.Microbiology and molecular biology reviews : MMBR · 2005
    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

3 authors at 2 institutions in 2 countries.

R RamakrishnanCurriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC 27599, USA.
M Schuster
R B Bourret
University of North Carolina at Chapel Hill · USInstitut thématique Génétique, génomique et bioinformatique · FR

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 GM50860NIGMS NIH HHS R01 GM050860
6 · The paper itself

Abstract

When Escherichia coli cells lacking all chemotaxis proteins except the response regulator CheY are exposed to acetate, clockwise flagellar rotation results, indicating the acetate stimulus has activated signaling by CheY. Acetate can be converted to acetyl-CoA by either of two different metabolic pathways, which proceed through acetyl phosphate or acetyl-AMP intermediates. In turn, CheY can be covalently modified by either intermediate in vitro, leading to phosphorylation or acetylation, respectively. Either pathway is sufficient to support the CheY-mediated response to acetate in vivo. Whereas phosphorylation of Asp-57 is a recognized mechanism for activation of CheY to stimulate clockwise flagellar rotation, acetylation of CheY is less well characterized. We found evidence for multiple CheY acetylation sites by mass spectrometry and directly identified Lys-92 and Lys-109 as acetylation sites by Edman degradation of peptides from [14C]acetate-labeled CheY. Replacement of CheY Lys-92, the preferred acetylation site, with Arg has little effect on chemotaxis but completely prevents the response to acetate via the acetyl-AMP pathway. Thus acetylation of Lys-92 activates clockwise signaling by CheY in vivo. The mechanism by which acetylation activates CheY apparently is not simple charge neutralization, nor does it involve enhanced binding to the FliM flagellar switch protein. Thus acetylation probably affects signal generation by CheY at a step after switch binding.

Indexed as

Bacterial ProteinsAcetate-CoA LigaseAcetylationChemotaxisEscherichia coliEscherichia coli ProteinsLysineMass SpectrometryMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsSaccharomyces cerevisiaeSignal TransductionStructure-Activity RelationshipAcetate-CoA LigaseBacterial ProteinscheY protein, E coliEscherichia coli ProteinsLysineMembrane ProteinsMethyl-Accepting Chemotaxis Proteins

Identifiers

PMID9560203
PMCPMC20188
OpenAlexW2160253279

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.