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Unique methionine-aromatic interactions govern the calmodulin redox sensor.

Daniel G Walgenbach1, Andrew J Gregory1, Jennifer C Klein1

  • 1University of Wisconsin-La Crosse, 1725 State Street, La Crosse, WI, USA.

Biochemical and Biophysical Research Communications
|September 24, 2018
PubMed
Summary

Oxidation of methionine in calmodulin alters its structure and function. This study reveals how redox-sensitive interactions control calmodulin

Keywords:
AgingCalmodulinMethionineOxidation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein that regulates numerous cellular targets.
  • CaM contains multiple methionine residues susceptible to oxidation, which impacts its regulatory functions.
  • Understanding the structural basis of CaM's redox sensitivity is vital for comprehending cellular signaling.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which calmodulin detects and responds to methionine oxidation.
  • To define the role of methionine-aromatic interactions in CaM's structural dynamics and redox sensing.
  • To investigate how mimicking methionine oxidation affects CaM's conformational transitions.

Main Methods:

  • Utilized molecular dynamics (MD) simulations to analyze CaM's structural dynamics.
  • Investigated the role of methionine-aromatic interactions in stabilizing CaM's open and closed states.
  • Employed site-directed mutagenesis, substituting methionine with glutamine to mimic oxidation.

Main Results:

  • Identified unique, redox-sensitive methionine-aromatic interactions stabilizing distinct CaM conformational states.
  • Demonstrated coupling between key methionine-aromatic interactions and EF hand helix reorientation.
  • Observed that methionine-to-glutamine substitutions significantly altered CaM's conformational transitions by modulating interaction strengths.

Conclusions:

  • Methionine oxidation in CaM alters functional dynamics by modulating the strength of critical methionine-aromatic interactions.
  • These findings suggest a general redox sensing mechanism involving methionine-aromatic interactions in proteins.
  • CaM's structural plasticity allows it to act as a sensor for cellular oxidative stress.