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Plant and Cell Physiology Advance Access originally published online on August 14, 2007
Plant and Cell Physiology 2007 48(9):1359-1373; doi:10.1093/pcp/pcm108
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Redox Regulation of Chloroplast Enzymes in Galdieria sulphuraria in View of Eukaryotic Evolution

Christine Oesterhelt1, Susanne Klocke2, Simone Holtgrefe2, Vera Linke2, Andreas P. M. Weber3 and Renate Scheibe2,*

1Department of Plant Physiology, Institute for Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24–25, D-14476 Potsdam-Golm, Germany
2Department of Plant Physiology, Faculty of Biology and Chemistry, University of Osnabrück, D-49069 Osnabrück, Germany
3Department of Plant Biochemistry, Heinrich-Heine-University, D-40225 Düsseldorf, Germany

*Corresponding author: E-mail, scheibe{at}biologie.uni-osnabrueck.de; Fax, +49-541-969-2265.


  Abstract

Redox modulation is a general mechanism for enzyme regulation, particularly for the post-translational regulation of the Calvin cycle in chloroplasts of green plants. Although red algae and photosynthetic protists that harbor plastids of red algal origin contribute greatly to global carbon fixation, relatively little is known about post-translational regulation of chloroplast enzymes in this important group of photosynthetic eukaryotes. To address this question, we used biochemistry, phylogenetics and analysis of recently completed genome sequences. We studied the functionality of the chloroplast enzymes phosphoribulokinase (PRK, EC 2.7.1.19 [EC] ), NADP-dependent glyceraldehyde 3-phosphate dehydrogenase (NADP-GAPDH, GapA, EC 1.2.1.13 [EC] ), fructose 1,6-bisphosphatase (FBPase, EC 3.1.3.1 [EC] 1) and glucose 6-phosphate dehydrogenase (G6PDH, EC 1.1.1.49 [EC] ), as well as NADP-malate dehydrogenase (NADP-MDH, EC 1.1.1.3 [EC] 7) in the unicellular red alga Galdieria sulphuraria (Galdieri) Merola. Despite high sequence similarity of G. sulphuraria proteins to those of other photosynthetic organisms, we found a number of distinct differences. Both PRK and GAPDH co-eluted with CP12 in a high molecular weight complex in the presence of oxidized glutathione, although Galdieria CP12 lacks the two cysteines essential for the formation of the N-terminal peptide loop present in higher plants. However, PRK inactivation upon complex formation turned out to be incomplete. G6PDH was redox modulated, but remained in its tetrameric form; FBPase was poorly redox regulated, despite conservation of the two redox-active cysteines. No indication for the presence of plastidic NADP-MDH (and other components of the malate valve) was found.

Keywords: Chloroplast enzymes - Complex formation - CP12 - Galdieria sulphuraria - Light/dark modulation - Molecular evolution

Abbreviations: BSA, bovine serum albumin; DTT, dithiothreitol; EST, expressed sequence tag; FBPase, fructose 1,6-bisphosphatase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; G6PDH, glucose 6-phosphate dehydrogenase; MDH, malate dehydrogenase; PRK, phosphoribulokinase; RT–PCR, reverse transcription–PCR.

(Received May 31, 2007; Accepted August 10, 2007)
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