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PMID: 8415608 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 19 ·1993-10-01 ·Pages 8787-91

Welch M, Oosawa K, Aizawa S, Eisenbach M

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.

MeSH Terms
Amides/pharmacology Bacterial Proteins/biosynthesis,isolation & purification,metabolism Chemotaxis/physiology Escherichia coli/metabolism Escherichia coli Proteins Flagella/metabolism,physiology Kinetics Leucine/metabolism Membrane Proteins/metabolism Methyl-Accepting Chemotaxis Proteins Organophosphates/pharmacology Phosphoric Acids/pharmacology Phosphorylation Protein Binding
Chemicals
Amides Bacterial Proteins Escherichia coli Proteins FliN protein, Bacteria Flig protein, Bacteria Membrane Proteins Methyl-Accepting Chemotaxis Proteins Organophosphates Phosphoric Acids cheY protein, E coli FliM protein, Bacteria acetyl phosphate phosphoramidic acid Leucine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Welch M
Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel.
Oosawa K
Aizawa S
Eisenbach M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.19.8787
Published
1993-10-01
Pages
8787-91
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC47445
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.90.19.8787 PMC Full Text View journal details
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