Modulation, via Protein-Protein Interactions, of Glyceraldehyde-3-phosphate Dehydrogenase Activity through Redox Phosphoribulokinase Regulation

Lebreton, Sandrine; Graciet, Emmanuelle; Gontero, Brigitte

doi:10.1074/jbc.m213096200

Cited by 48 publications

(47 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is consistent with previous studies that demonstrated a role for this complex in the regulation of PRK activity (13,17,20,30,33). In the dark, the thioredoxin-activated Calvin cycle enzymes, including PRK and GAPDH, have been shown to be inactive and it has been assumed that this deactivation results from the formation of the oxidized state of the enzyme (3,27,34).…”

Section: Discussionsupporting

confidence: 80%

“…It has been hypothesized that the function of the PRK/GAPDH/CP12 complex is to provide an additional mode of light/dark regulation of the Calvin cycle mediated by changes in the levels of NADP(H) (16). Much of our more recent knowledge about this complex has been gained from studies on in vitro coexpression of PRK, CP12 and the GapA subunit of GAPDH (13,17,(19)(20)(21), which has led to the proposal that the function of the PRK/GAPDH/CP12 even in higher plants, is to provide redox control of the A 4 GAPDH isoform (21). However, in contrast to algae, in higher plants the most abundant and active form of chloroplastic GAPDH is a heterotetramer, containing two distinct subunits, GapA and GapB.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability

Howard

Metodiev

Lloyd

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

106

133

View full text Add to dashboard Cite

A Calvin cycle multiprotein complex including phosphoribulokinase (PRK), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and a small protein, CP12, has previously been identified. In this article, we have studied this complex in leaves and have shown that dissociation and reassociation of the PRK/GAPDH/CP12 complex occurs in a time frame of minutes, allowing for rapid regulation of enzyme activity. Furthermore, we have shown that the extent of formation and dissociation of the PRK/GAPDH/CP12 complex correlates with the quantity of light. These data provide evidence linking the status of this complex with the rapid and subtle regulation of GAPDH and PRK activities in response to fluctuations in light availability. We have also demonstrated that dissociation of this complex depends on electron transport chain activity and that the major factor involved in the dissociation of the pea complex was thioredoxin f. We show here that both PRK and GAPDH are present in the reduced form in leaves in the dark, but are inactive, demonstrating the role of the PRK/GAPDH/CP12 complex in deactivating these enzymes in response to reductions in light intensity. Based on our data, we propose a model for thioredoxin f-mediated activation of PRK and GAPDH by two mechanisms: directly through reduction of disulfide bonds within these enzymes and indirectly by mediating the breakdown of the complex in response to changes in light intensity.Calvin cycle ͉ photosynthesis ͉ protein-protein interactions ͉ redox

show abstract

Section: Discussionsupporting

confidence: 80%

mentioning

confidence: 99%

Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability

Howard

Metodiev

Lloyd

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

106

133

View full text Add to dashboard Cite

show abstract

“…The association behavior and activity of this AB isoform is redox-regulated by Trx-f. In addition, regulation by the protein factor CP12 as well as by NAD and 1,3-bisphosphoglycerate has also been reported (Wedel and Soll 1998;Lebreton and Gontero 1999;Lebreton et al 2003). These factors have an effect on the oligomerization state of the enzyme and on its association with phophoribulokinase, another Calvin-cycle enzyme.…”

Section: Glyceraldehyde-3 Phosphate Dehydrogenasementioning

confidence: 96%

Structural Basis of Redox Signaling in Photosynthesis: Structure and Function of Ferredoxin:thioredoxin Reductase and Target Enzymes

Dai

Johansson

Miginiac‐Maslow

et al. 2004

Photosynthesis Research

View full text Add to dashboard Cite

The role of the ferredoxin:thioredoxin system in the reversible light activation of chloroplast enzymes by thioldisulfide interchange with thioredoxins is now well established. Recent fruitful collaboration between biochemists and structural biologists, reflected by the shared authorship of the paper, allowed to solve the structures of all of the components of the system, including several target enzymes, thus providing a structural basis for the elucidation of the activation mechanism at a molecular level. In the present Review, these structural data are analyzed in conjunction with the information that was obtained previously through biochemical and site-directed mutagenesis approaches. The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms. Thioredoxins in turn reduce regulatory disulfides of various target enzymes. This process triggers conformational changes on these enzymes, allowing them to reach optimal activity. No common activation mechanism can be put forward for these enzymes, as every thioredoxin-regulated protein undergoes specific structural modifications. It is thus important to solve the structures of the individual target enzymes in order to fully understand the molecular mechanism of the redox regulation of each of them.Abbreviations: FBPase -fructose-

show abstract

“…SPR studies with immobilized reduced PRK (ligand), and different concentrations of native GAPDH (GAPDH/CP12) (analyte) have shown that the dissociation constant (K d ) of the native GAPDH/PRK association is 62 nM (22). We determined the dissociation constants of different subcomplexes by SPR to find how oxidized CP12 acts in complex assembly.…”

Section: Reinhardtii Cp12 Is Similar To Higher Plant Cp12mentioning

confidence: 99%

The Small Protein CP12: A Protein Linker for Supramolecular Complex Assembly

et al. 2003

Self Cite

View full text Add to dashboard Cite

CP12 is an 8.5-kDa nuclear-encoded chloroplast protein, isolated from higher plants. It forms part of a core complex of two dimers of phosphoribulokinase (PRK), two tetramers of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and CP12. The role of CP12 in this complex assembly has not been determined. To address this question, we cloned a cDNA encoding the mature CP12 from the green alga Chlamydomonas reinhardtii and expressed it in Escherichia coli. Sequence alignments show that it is very similar to other CP12s, with four conserved cysteine residues forming two disulfide bridges in the oxidized CP12. On the basis of reconstitution assays and surface plasmon resonance binding studies, we show that oxidized, but not reduced, CP12 acts as a linker in the assembly of the complex, and we propose a model in which CP12 associates with GAPDH, causing its conformation to change. This GAPDH/ CP12 complex binds PRK to form a half-complex (one unit). This unit probably dimerizes due partially to interactions between the enzymes of each unit. Reduced CP12 being unable to reconstitute the complex, we studied the structures of oxidized and reduced CP12 by NMR and circular dichroism to determine whether reduction induced structural transitions. Oxidized CP12 is mainly composed of R helix and coil segments, and is extremely flexible, while reduced CP12 is mainly unstructured. Remarkably, CP12 has similar physicochemical properties to those of "intrinsically unstructured proteins" that are also involved in regulating macromolecular complexes, or in their assembly. CP12s are thus one of the few protein families of intrinsically unstructured proteins specific to plants.

show abstract

Modulation, via Protein-Protein Interactions, of Glyceraldehyde-3-phosphate Dehydrogenase Activity through Redox Phosphoribulokinase Regulation

Cited by 48 publications

References 45 publications

Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability

Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability

Structural Basis of Redox Signaling in Photosynthesis: Structure and Function of Ferredoxin:thioredoxin Reductase and Target Enzymes

The Small Protein CP12: A Protein Linker for Supramolecular Complex Assembly

Contact Info

Product

Resources

About