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Related Experiment Videos

Conformational coupling in the chemotaxis response regulator CheY.

M Schuster1, R E Silversmith, R B Bourret

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

Proceedings of the National Academy of Sciences of the United States of America
|May 17, 2001
PubMed
Summary

Bacterial chemotaxis protein CheY

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • CheY is a key response regulator in bacterial chemotaxis, central to two-component signal transduction.
  • Its phosphorylation at the active site causes conformational changes affecting interactions with motor proteins (FliM), kinases (CheA), and phosphatases (CheZ).

Purpose of the Study:

  • To investigate the reverse conformational coupling between CheY's phosphorylation site and its signaling surface.
  • To quantify CheY phosphorylation activity influenced by interacting proteins.

Main Methods:

  • Assessing CheY autophosphorylation kinetics with phosphodonors.
  • Analyzing the impact of specific CheA, CheZ, and FliM peptide binding on CheY phosphorylation.
  • Characterizing CheY mutants to identify key residues in conformational coupling.

Main Results:

  • Peptide binding of CheA, CheZ, and FliM significantly altered CheY autophosphorylation, indicating reverse signal propagation.
  • Autodephosphorylation rates and substrate affinity of CheY were largely unaffected by peptide binding.
  • Specific residues (Thr-87, Tyr-106, Lys-109) previously linked to activation were not essential for this reverse conformational coupling.

Conclusions:

  • CheY exhibits reverse signal propagation, where interactions at the signaling surface influence phosphorylation.
  • Findings support a multistate thermodynamic model for response regulator activation.
  • Provides structural and mechanistic insights into CheY function in chemotaxis.

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