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Related Experiment Videos

Throwing the switch in bacterial chemotaxis.

R E Silversmith1, R B Bourret

  • 1Dept of Microbiology and Immunology, University of North Carolina, Chapel Hill 27599-7290, USA.

Trends in Microbiology
|March 9, 1999
PubMed
Summary

Phosphorylation of CheY protein in Escherichia coli triggers flagellar motor switching. Analysis of CheY variants reveals conformational changes enabling interaction with the flagellum, but the timing of binding and switching remains unclear.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Escherichia coli uses chemotaxis to navigate environments.
  • Flagellar rotation direction dictates bacterial movement (counterclockwise for forward, clockwise for tumbling).
  • The CheY protein, upon phosphorylation, is the key signal transducer in this process.

Purpose of the Study:

  • To investigate the molecular mechanisms of flagellar switching in E. coli chemotaxis.
  • To understand how phosphorylated CheY interacts with the flagellar motor.
  • To elucidate the relationship between phospho-CheY binding and flagellar switching events.

Main Methods:

  • Analysis of various CheY protein variants.
  • Studying conformational changes in CheY upon phosphorylation.

Related Experiment Videos

  • Investigating the interaction of CheY with the flagellar base.

    • Main Results:

    • Specific surfaces of CheY undergo conformational changes after phosphorylation.
    • These altered surfaces are crucial for direct interaction with the flagellar apparatus.
    • The study provides insights into the structural basis of CheY's function.

    Conclusions:

    • Phosphorylated CheY directly interacts with the flagellum to mediate motor switching.
    • The precise temporal relationship between phospho-CheY binding and flagellar switching requires further investigation.
    • Further research is needed to determine if binding and switching are sequential or concerted.