TAILIEUCHUNG - Báo cáo khoa học: The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation

In animal cells, many proteins have been shown to undergo glutathionyla-tion under conditions of oxidative stress. By contrast, very little is known about this post-translational modification in plants. In the present work, we showed, using mass spectrometry, that the recombinant chloroplast A4-glyceraldehyde-3-phosphate dehydrogenase (A4-GAPDH) from Arabid-opsis thaliana is glutathionylated with either oxidized glutathione or reduced glutathione and H2O2. | ễFEBS Journal The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation Mirko Zaffagnini1 2 Laure Michelet2 Christophe Marchand3 Francesca Sparla1 Paulette Decottignies3 Pierre Le Marechal3 Myroslawa Miginiac-Maslow2 Graham Noctor2 Paolo Trost1 and Stephane D. Lemaire2 1 Laboratory of Molecular Plant Physiology University of Bologna Italy 2 Institut de Biotechnologie des Plantes UMR 8618 CNRS Université Paris-Sud Orsay France 3 Institut de Biochimie et Biophysique Moleculaire et Cellulaire CNRS Universite Paris-Sud Orsay France Keywords Arabidopsis thaliana Calvin cycle GAPDH glutathionylation oxidative stress Correspondence S. D. Lemaire Institut de Biotechnologie des Plantes Batiment 630 Universite Paris-Sud F-91405 Orsay Cedex France Fax 33 1 69153423 Tel. 33 1 69153338 E-mail Received 3 October 2006 revised 25 October 2006 accepted 7 November 2006 doi In animal cells many proteins have been shown to undergo glutathionyla-tion under conditions of oxidative stress. By contrast very little is known about this post-translational modification in plants. In the present work we showed using mass spectrometry that the recombinant chloroplast A4-glyceraldehyde-3-phosphate dehydrogenase A4-GAPDH from Arabid-opsis thaliana is glutathionylated with either oxidized glutathione or reduced glutathione and H2O2. The formation of a mixed disulfide between glutathione and A4-GAPDH resulted in the inhibition of enzyme activity. A4-GAPDH was also inhibited by oxidants such as H2O2. However the effect of glutathionylation was reversed by reductants whereas oxidation resulted in irreversible enzyme inactivation. On the other hand the major isoform of photosynthetic GAPDH of higher plants . the AnBn-GAPDH isozyme in either A2B2 or A8B8 conformation was sensitive to oxidants but did not seem to undergo glutathionylation significantly. GAPDH .

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