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Glutaredoxin s12: unique properties for redox signaling.

Mirko Zaffagnini1, Mariette Bedhomme, Christophe H Marchand

  • 1Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, FRE3354 Centre National de la Recherche Scientifique, Institut de Biologie Physico-Chimique, Université Pierre et Marie Curies, Paris, France.

Antioxidants & Redox Signaling
|June 29, 2011
PubMed
Summary

Poplar chloroplast glutaredoxin GrxS12 acts as a redox sensor. Its glutathionylation, influenced by light and stress, allows glutathione to signal through target proteins.

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Published on: June 18, 2020

Area of Science:

  • Plant biochemistry
  • Redox biology
  • Molecular plant science

Background:

  • Cysteine residues in proteins can be modified by oxidation.
  • Glutathionylation, a post-translational modification, involves the reaction of reduced glutathione (GSH) with oxidized cysteines.
  • Glutaredoxins (Grx) catalyze the reverse reaction, deglutathionylation, often requiring GSH.

Purpose of the Study:

  • To investigate the catalytic and thermodynamic properties of poplar chloroplast GrxS12.
  • To understand the role of GrxS12 in redox sensing and signaling within chloroplasts.
  • To explore the impact of environmental conditions (light, stress) on GrxS12 activity.

Main Methods:

  • Characterization of GrxS12's reaction with glutathionylated substrates.
  • Determination of the pK(a) of the catalytic cysteine in GrxS12.
  • Thermodynamic analysis of the equilibrium between GrxS12 and glutathione (GSH).
  • Assessment of GrxS12 sensitivity to oxidation and direct glutathionylation.

Main Results:

  • Poplar chloroplast GrxS12 efficiently catalyzes deglutathionylation in a GSH-dependent manner.
  • GrxS12 possesses a low pK(a) (3.9) for its catalytic cysteine, rendering it susceptible to oxidation and glutathionylation.
  • Glutathionylated GrxS12 (GrxS12-SSG) is inactive until deglutathionylated by GSH.
  • The redox equilibrium of GrxS12 favors oxidation under dark conditions (pH 7.0) compared to illuminated conditions (pH 7.9).

Conclusions:

  • GrxS12's unique properties suggest its function as a stress-related redox sensor in chloroplasts.
  • Accumulation of GrxS12-SSG is predicted under mild oxidative stress.
  • GrxS12 may mediate glutathione's signaling role by modulating glutathionylation of target proteins.