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. 1993 Oct 1;90(19):8787–8791. doi: 10.1073/pnas.90.19.8787

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

M Welch 1, K Oosawa 1, S Aizawa 1, M Eisenbach 1
PMCID: PMC47445  PMID: 8415608

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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