Photosynthesis Research

, Volume 89, Issue 2–3, pp 263–275 | Cite as

Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms

  • P. Trost
  • S. Fermani
  • L. Marri
  • M. Zaffagnini
  • G. Falini
  • S. Scagliarini
  • P. Pupillo
  • F. Sparla


Regulation of the Calvin–Benson cycle under varying light/dark conditions is a common property of oxygenic photosynthetic organisms and photosynthetic glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is one of the targets of this complex regulatory system. In cyanobacteria and most algae, photosynthetic GAPDH is a homotetramer of GapA subunits which do not contain regulatory domains. In these organisms, dark-inhibition of the Calvin–Benson cycle involves the formation of a kinetically inhibited supramolecular complex between GAPDH, the regulatory peptide CP12 and phosphoribulokinase. Conditions prevailing in the dark, i.e. oxidation of thioredoxins and low NADP(H)/NAD(H) ratio promote aggregation. Although this regulatory system has been inherited in higher plants, these phototrophs contain in addition a second type of GAPDH subunits (GapB) resulting from the fusion of GapA with the C-terminal half of CP12. Heterotetrameric A2B2-GAPDH constitutes the major photosynthetic GAPDH isoform of higher plants chloroplasts and coexists with CP12 and A4-GAPDH. GapB subunits of A2B2-GAPDH have inherited from CP12 a regulatory domain (CTE for C-terminal extension) which makes the enzyme sensitive to thioredoxins and pyridine nucleotides, resembling the GAPDH/CP12/PRK system. The two systems are similar in other respects: oxidizing conditions and low NADP(H)/NAD(H) ratios promote aggregation of A2B2-GAPDH into strongly inactivated A8B8-GAPDH hexadecamers, and both CP12 and CTE specifically affect the NADPH-dependent activity of GAPDH. The alternative, lower activity with NADH is always unaffected. Based on the crystal structure of spinach A4-GAPDH and the analysis of site-specific mutants, a model of the autonomous (CP12-independent) regulatory mechanism of A2B2-GAPDH is proposed. Both CP12 and CTE seem to regulate different photosynthetic GAPDH isoforms according to a common and ancient molecular mechanism.


Calvin-Benson cycle Disulfide Light/dark regulation Pyridine nucleotides Supramolecular complex Thioredoxin 





C-terminal extension of subunits GapB

GapA and GapB

subunits A and B, respectively, of photosynthetic glyceraldehyde-3-phosphate dehydrogenase


glyceraldehyde-3-phosphate dehydrogenase


NADP-dependent malate dehydrogenase





Work in the laboratory of the authors has been supported by the Italian Ministry of University (grants FIRB 2004 and PRIN 2005).


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Copyright information

© Springer Science+Business Media B.V. 2006

Authors and Affiliations

  • P. Trost
    • 1
  • S. Fermani
    • 2
  • L. Marri
    • 1
  • M. Zaffagnini
    • 1
  • G. Falini
    • 2
  • S. Scagliarini
    • 1
  • P. Pupillo
    • 1
  • F. Sparla
    • 1
  1. 1.Laboratory of Molecular Plant Physiology, Department of Evolutionary Experimental BiologyUniversity of BolognaBolognaItaly
  2. 2.Department of Chemistry “G. Ciamician”University of BolognaBolognaItaly

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