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Literature DB >> 19358329

A molecular mechanism of bacterial flagellar motor switching.

Collin M Dyer¹, Armand S Vartanian, Hongjun Zhou, Frederick W Dahlquist.

Abstract

The high-resolution structures of nearly all the proteins that comprise the bacterial flagellar motor switch complex have been solved; yet a clear picture of the switching mechanism has not emerged. Here, we used NMR to characterize the interaction modes and solution properties of a number of these proteins, including several soluble fragments of the flagellar motor proteins FliM and FliG, and the response-regulator CheY. We find that activated CheY, the switch signal, binds to a previously unidentified region of FliM, adjacent to the FliM-FliM interface. We also find that activated CheY and FliG bind with mutual exclusivity to this site on FliM, because their respective binding surfaces partially overlap. These data support a model of CheY-driven motor switching wherein the binding of activated CheY to FliM displaces the carboxy-terminal domain of FliG (FliGC) from FliM, modulating the FliGC-MotA interaction, and causing the motor to switch rotational sense as required for chemotaxis.

Entities: CellLine Chemical Disease Gene Mutation Species

Mesh：

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Year: 2009 PMID： 19358329 PMCID： PMC3327947 DOI： 10.1016/j.jmb.2009.02.004

Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469

54 in total

1. Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor.

Authors: S A Lloyd; F G Whitby; D F Blair; C P Hill
Journal: Nature Date: 1999-07-29 Impact factor: 49.962

2. Efficient adaptational demethylation of chemoreceptors requires the same enzyme-docking site as efficient methylation.

Authors: A N Barnakov; L A Barnakova; G L Hazelbauer
Journal: Proc Natl Acad Sci U S A Date: 1999-09-14 Impact factor: 11.205

3. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM.

Authors: M M McEvoy; A Bren; M Eisenbach; F W Dahlquist
Journal: J Mol Biol Date: 1999-06-25 Impact factor: 5.469

4. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Authors: J MONOD; J WYMAN; J P CHANGEUX
Journal: J Mol Biol Date: 1965-05 Impact factor: 5.469

5. Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX.

Authors: Sang-Youn Park; Xingjuan Chao; Gabriela Gonzalez-Bonet; Bryan D Beel; Alexandrine M Bilwes; Brian R Crane
Journal: Mol Cell Date: 2004-11-19 Impact factor: 17.970

6. Single-cell FRET imaging of phosphatase activity in the Escherichia coli chemotaxis system.

Authors: Ady Vaknin; Howard C Berg
Journal: Proc Natl Acad Sci U S A Date: 2004-11-29 Impact factor: 11.205

7. Domain analysis of the FliM protein of Escherichia coli.

Authors: M A Mathews; H L Tang; D F Blair
Journal: J Bacteriol Date: 1998-11 Impact factor: 3.490

8. The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY.

Authors: A Bren; M Eisenbach
Journal: J Mol Biol Date: 1998-05-08 Impact factor: 5.469

9. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima.

Authors: Perry N Brown; Michael A A Mathews; Lisa A Joss; Christopher P Hill; David F Blair
Journal: J Bacteriol Date: 2005-04 Impact factor: 3.490

10. Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.

Authors: K C Usher; A F de la Cruz; F W Dahlquist; R V Swanson; M I Simon; S J Remington
Journal: Protein Sci Date: 1998-02 Impact factor: 6.725

43 in total

A molecular mechanism of bacterial flagellar motor switching.

1. Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor.

2. Efficient adaptational demethylation of chemoreceptors requires the same enzyme-docking site as efficient methylation.

3. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM.

4. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

5. Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX.

6. Single-cell FRET imaging of phosphatase activity in the Escherichia coli chemotaxis system.

7. Domain analysis of the FliM protein of Escherichia coli.

8. The N terminus of the flagellar switch protein, FliM, is the binding domain for the chemotactic response regulator, CheY.

9. Crystal structure of the flagellar rotor protein FliN from Thermotoga maritima.

10. Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.

1. A molecular mechanism of direction switching in the flagellar motor of Escherichia coli.

2. Evidence for symmetry in the elementary process of bidirectional torque generation by the bacterial flagellar motor.

3. Structure of flagellar motor proteins in complex allows for insights into motor structure and switching.

4. Bacterial flagellar switching: a molecular mechanism directed by the logic of an electric motor.

5. Subunit organization and reversal-associated movements in the flagellar switch of Escherichia coli.

6. Architecture of the flagellar rotor.

Review 7. Signal processing in complex chemotaxis pathways.

Review 8. Nutrient-sensing mechanisms across evolution.

9. Organization of the Flagellar Switch Complex of Bacillus subtilis.

10. Structure and activity of the flagellar rotor protein FliY: a member of the CheC phosphatase family.