Evidence map›Paper›PMID 33620739›Full record

ArticleThe EMBO journal2021

The switching mechanism of the bacterial rotary motor combines tight regulation with inherent flexibility.

Oshri Afanzar, Diana Di Paolo, Miriam Eisenstein, Kohava Levi, Anne Plochowietz, Achillefs N Kapanidis, Richard Michael Berry, Michael Eisenbach

Abstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Speed-dependent bacterial surface swimming.Applied and environmental microbiology · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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

8 authors.

Oshri AfanzarDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-9690-3180
Diana Di PaoloBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Miriam EisensteinDepartment of Chemical Research Support, The Weizmann Institute of Science, Rehovot, Israel.
Kohava LeviDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Anne PlochowietzBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Achillefs N KapanidisBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Richard Michael BerryBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.
Michael EisenbachDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-9048-4720

Funding

Biotechnology and Biological Sciences Research Council BB/H01795X/1
6 · The paper itself

Abstract

Regulatory switches are wide spread in many biological systems. Uniquely among them, the switch of the bacterial flagellar motor is not an on/off switch but rather controls the motor's direction of rotation in response to binding of the signaling protein CheY. Despite its extensive study, the molecular mechanism underlying this switch has remained largely unclear. Here, we resolved the functions of each of the three CheY-binding sites at the switch in E. coli, as well as their different dependencies on phosphorylation and acetylation of CheY. Based on this, we propose that CheY motor switching activity is potentiated upon binding to the first site. Binding of potentiated CheY to the second site produces unstable switching and at the same time enables CheY binding to the third site, an event that stabilizes the switched state. Thereby, this mechanism exemplifies a unique combination of tight motor regulation with inherent switching flexibility.

Indexed as

Bacterial ProteinsEscherichia coliEscherichia coli ProteinsFlagellaLocomotionMethyl-Accepting Chemotaxis ProteinsMolecular Motor ProteinsProtein BindingBacterial ProteinscheY protein, E coliEscherichia coli ProteinsFliM protein, BacteriaMethyl-Accepting Chemotaxis ProteinsMolecular Motor Proteinsacetylated CheYbacterial chemotaxisbacterial flagellar motorflagellar switchmolecular switch

Identifiers

PMID33620739
PMCPMC7957414

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.