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Cited by 423

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Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria.

Open access
Welch, M, Oosawa, K, Aizawa, S, Eisenbach, M·1993·Proceedings of the National Academy of Sciences

Abstract

Regulation of the direction of flagellar rotation is central to the mechanism of bacterial chemotaxis. The transitions between counterclockwise and clockwise rotation are controlled by a "switch complex" composed of three proteins (FliG, FliM, and FliN) and located at the base of the flagellar motor. The mechanism of function of the switch is unknown. Here we demonstrate that the diffusible clockwise-signal molecule, the CheY protein, binds to the switch, that the primary docking site is FliM, that the extent of CheY binding to FliM is dependent upon the phosphorylation level of CheY, and that it is unaffected by the other two switch proteins. This study provides a biochemical demonstration of binding of a signal molecule to the bacterial switch and demonstrates directly that phosphorylation regulates the activity of this molecule.

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Metadata

Authors
Welch, M., Oosawa, K., Aizawa, S., & Eisenbach, M.
Venue
Proceedings of the National Academy of Sciences
Published
1993-10
Volume
90
Issue
19
Pages
8787-8791
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2049716406
Cited by
423
References
0
FWCI
8.50
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. https://app.cochat.ai/papers/10.1073/pnas.90.19.8787
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Welch, M., Oosawa, K., Aizawa, S., & Eisenbach, M. (1993). Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.19.8787

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.