Evidence map›Paper›PMID 25388160›Full record

ArticleMolecular microbiology2015

CheY's acetylation sites responsible for generating clockwise flagellar rotation in Escherichia coli.

Milana Fraiberg, Oshri Afanzar, C Keith Cassidy, Alexandra Gabashvili, Klaus Schulten, Yishai Levin, Michael Eisenbach

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  3. Contribution of NmSystems · 2021
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  7. Review
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  12. Structure and function of the archaeal response regulator CheY.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
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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

7 authors at 2 institutions in 2 countries.

Milana FraibergDepartment of Biological Chemistry, The Weizmann Institute of Science, 7610001, Rehovot, Israel.
Oshri Afanzar
C Keith Cassidy
Alexandra Gabashvili
Klaus Schulten
Yishai Levin
Michael Eisenbach
Weizmann Institute of Science · ILUniversity of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Intramural NIH HHSNIGMS NIH HHS 9P41GM104601NIGMS NIH HHS P41 GM104601
6 · The paper itself

Abstract

Stimulation of Escherichia coli with acetate elevates the acetylation level of the chemotaxis response regulator CheY. This elevation, in an unknown mechanism, activates CheY to generate clockwise rotation. Here, using quantitative selective reaction monitoring mass spectrometry and high-resolution targeted mass spectrometry, we identified K91 and K109 as the major sites whose acetylation level in vivo increases in response to acetate. Employing single and multiple lysine replacements in CheY, we found that K91 and K109 are also the sites mainly responsible for acetate-dependent clockwise generation. Furthermore, we showed that clockwise rotation is repressed when residue K91 is nonmodified, as evidenced by an increased ability of CheY to generate clockwise rotation when K91 was acetylated or replaced by specific amino acids. Using molecular dynamics simulations, we show that K91 repression is manifested in the conformational dynamics of the β4α4 loop, shifted toward an active state upon mutation. Removal of β4α4 loop repression may represent a general activation mechanism in CheY, pertaining also to the canonical phosphorylation activation pathway as suggested by crystal structures of active and inactive CheY from Thermotoga maritima. By way of elimination, we further suggest that K109 acetylation is actively involved in generating clockwise rotation.

Indexed as

AcetatesAcetylationBacterial ProteinsChemotaxisEscherichia coliEscherichia coli ProteinsLysineMass SpectrometryMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular Dynamics SimulationProtein Processing, Post-TranslationalProtein Structure, TertiarySequence Analysis, ProteinThermotoga maritimaAcetatesBacterial ProteinscheY protein, E coliEscherichia coli ProteinsLysineMembrane ProteinsMethyl-Accepting Chemotaxis Proteins

Identifiers

PMID25388160
PMCPMC4426874
OpenAlexW1887060892

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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.