FEBS Letters
Volume 584, Issue 11 , Pages 2242-2248, 3 June 2010

Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii: Kinetics and specificity in deglutathionylation reactions

Edited by Richard Cogdell

  • Xing-Huang Gao

      Affiliations

    • Institut de Biologie des Plantes, UMR 8618, CNRS/Univ Paris-Sud, Bâtiment 630, F-91405 Orsay Cedex, France
    • ,
  • Mirko Zaffagnini

      Affiliations

    • Institut de Biologie des Plantes, UMR 8618, CNRS/Univ Paris-Sud, Bâtiment 630, F-91405 Orsay Cedex, France
    • Present address: Laboratory of Molecular Plant Physiology, Department of Experimental Evolutionary Biology, University of Bologna, Bologna, Italy.
    • ,
  • Mariette Bedhomme

      Affiliations

    • Institut de Biologie des Plantes, UMR 8618, CNRS/Univ Paris-Sud, Bâtiment 630, F-91405 Orsay Cedex, France
    • ,
  • Laure Michelet

      Affiliations

    • Institut de Biologie des Plantes, UMR 8618, CNRS/Univ Paris-Sud, Bâtiment 630, F-91405 Orsay Cedex, France
    • ,
  • Corinne Cassier-Chauvat

      Affiliations

    • CEA, iBiTec-S, SBIGeM, LBI, CNRS URA 2096, Bat 142 CEA-Saclay, F-91191 Gif sur Yvette Cedex, France
    • ,
  • Paulette Decottignies

      Affiliations

    • Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619, CNRS/Univ Paris-Sud, Bâtiment 430, 91405 Orsay Cedex, France
    • ,
  • Stéphane D. Lemaire

      Affiliations

    • Institut de Biologie des Plantes, UMR 8618, CNRS/Univ Paris-Sud, Bâtiment 630, F-91405 Orsay Cedex, France
    • Corresponding Author InformationCorresponding author. Fax: +33 1 69 15 34 24.

Received 18 March 2010; received in revised form 9 April 2010; accepted 12 April 2010. published online 19 April 2010.

Abstract 

Protein deglutathionylation is mainly catalyzed by glutaredoxins (GRXs). We have analyzed the biochemical properties of four of the six different GRXs of Chlamydomonas reinhardtii. Kinetic parameters were determined for disulfide and dehydroascorbate reduction but also for deglutathionylation of artificial and protein substrates. The results indicate that GRXs exhibit striking differences in their catalytic properties, mainly linked to the class of GRX considered but also to the pKa of the N-terminal catalytic cysteine. Furthermore, glutathionylated proteins were found to exhibit distinct reactivities with GRXs. These results suggest that glutathionylation may allow a fine tuning of cell metabolism under stress conditions.

Structured summary

MINT-7761120: GRX6 (uniprotkb:A8HN52) and GRX6 (uniprotkb:A8HN52) bind (MI:0408) by comigration in non denaturing gel electrophoresis (MI:0404)

MINT-7761098:GRX5 (uniprotkb:A8I7Q4) and GRX5 (uniprotkb:A8I7Q4) bind (MI:0408) by comigration in non denaturing gel electrophoresis (MI:0404)

Abbreviations: A4-GAPDH, A4-glyceraldehyde-3-phosphate dehydrogenase, DHAR, dehydroascorbate reductase, GRX, glutaredoxin, GSH, reduced glutathione, ICL, isocitrate lyase

Keywords: Glutaredoxin, Glutathionylation, Redox signaling, Chlamydomonas reinhardtii

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PII: S0014-5793(10)00304-2

doi:10.1016/j.febslet.2010.04.034

FEBS Letters
Volume 584, Issue 11 , Pages 2242-2248, 3 June 2010

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