Regulation of glyceraldehyde-3-phosphate dehydrogenase in the eustigmatophyte<i>Pseudocharaciopsis ovalis</i>is intermediate between a chlorophyte and a diatom

Avilán, Luisana; Maberly, Stephen C.; Mekhalfi, Malika; Plateau, Julia; Puppo, Carine; Gontero, Brigitte

doi:10.1080/09670262.2012.687459

Cited by 6 publications

(5 citation statements)

References 48 publications

(62 reference statements)

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“…The eukaryotic green alga, Chlamydomonas reinhardtii , is a well-known biological model, and has been extensively studied and referred to as the photosynthetic yeast 38 . There are only a few IDPs reported from this green alga, such as the Chloroplast Protein (CP12), which forms a supramolecular complex with two key Calvin-Benson-Bassham (CBB) cycle enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK) 39 – 42 . This protein regulates the association–dissociation of this complex, thereby allowing the CBB cycle to be inactive in the dark and active in the light, but has moonlighting activities 43 , for instance, chaperone function 44 and metal ions binding 45 .…”

Section: Introductionmentioning

confidence: 99%

Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii

Zhang

Launay

Schramm

et al. 2018

Sci Rep

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The content of intrinsically disordered protein (IDP) is related to organism complexity, evolution, and regulation. In the Plantae, despite their high complexity, experimental investigation of IDP content is lacking. We identified by mass spectrometry 682 heat-resistant proteins from the green alga, Chlamydomonas reinhardtii. Using a phosphoproteome database, we found that 331 of these proteins are targets of phosphorylation. We analyzed the flexibility propensity of the heat-resistant proteins and their specific features as well as those of predicted IDPs from the same organism. Their mean percentage of disorder was about 20%. Most of the IDPs (~70%) were addressed to other compartments than mitochondrion and chloroplast. Their amino acid composition was biased compared to other classic IDPs. Their molecular functions were diverse; the predominant ones were nucleic acid binding and unfolded protein binding and the less abundant one was catalytic activity. The most represented proteins were ribosomal proteins, proteins associated to flagella, chaperones and histones. We also found CP12, the only experimental IDP from C. reinhardtii that is referenced in disordered protein database. This is the first experimental investigation of IDPs in C. reinhardtii that also combines in silico analysis.

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Section: Introductionmentioning

confidence: 99%

Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii

Zhang

Launay

Schramm

et al. 2018

Sci Rep

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“…One of the few studies of the effect of pH on enzyme activity in chromalveolates is for the chloroplastic glyceraldehyde-3-phosphate dehydrogenase (GAPDH) that catalyzes the reversible reduction and dephosphorylation of 1,3-bisphosphoglycerate to produce glyceraldehyde-3-phosphate and inorganic phosphate. Avilan et al ( Avilan et al, 2012 ) compared the optimal pH of GAPDH in the freshwater diatom, Asterionella formosa , the freshwater eustigmatophyte, Pseudocharaciopsis ovalis , and the model green alga, C. reinhardtii . In A. formosa , GAPDH was still active at the pH occurring in the dark, assuming that the internal pH (pH 7) reflects the one in the chloroplast.…”

Section: Regulation Of Photosynthesis By Light and Darkmentioning

confidence: 99%

Regulation of Carbon Metabolism by Environmental Conditions: A Perspective From Diatoms and Other Chromalveolates

et al. 2020

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Diatoms belong to a major, diverse and species-rich eukaryotic clade, the Heterokonta, within the polyphyletic chromalveolates. They evolved as a result of secondary endosymbiosis with one or more Plantae ancestors, but their precise evolutionary history is enigmatic. Nevertheless, this has conferred them with unique structural and biochemical properties that have allowed them to flourish in a wide range of different environments and cope with highly variable conditions. We review the effect of pH, light and dark, and CO 2 concentration on the regulation of carbon uptake and assimilation. We discuss the regulation of the Calvin-Benson-Bassham cycle, glycolysis, lipid synthesis, and carbohydrate synthesis at the level of gene transcripts (transcriptomics), proteins (proteomics) and enzyme activity. In contrast to Viridiplantae where redox regulation of metabolic enzymes is important, it appears to be less common in diatoms, based on the current evidence, but regulation at the transcriptional level seems to be widespread. The role of post-translational modifications such as phosphorylation, glutathionylation, etc., and of protein-protein interactions, has been overlooked and should be investigated further. Diatoms and other chromalveolates are understudied compared to the Viridiplantae, especially given their ecological importance, but we believe that the ever-growing number of sequenced genomes combined with proteomics, metabolomics, enzyme measurements, and the application of novel techniques will provide a better understanding of how this important group of algae maintain their productivity under changing conditions.

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“…However, the existence of the GAPDH–CP12–FNR complex explains the previously observed inhibition of GAPDH by NADPH in diatoms and other chromalveolates, a broad group including chrysophytes, cryptophytes, haptophytes and dinoflagellates, under oxidizing conditions (Boggetto et al ., ; Maberly et al ., ; Avilan et al ., ). It is well known that supramolecular complex formation results in the modification of the kinetic properties of proteins embedded within these edifices (Rault et al ., ; Gontero et al ., ).…”

Section: Discussionmentioning

confidence: 97%

Glyceraldehyde‐3‐phosphate dehydrogenase is regulated by ferredoxin‐NADP reductase in the diatom Asterionella formosa

et al. 2014

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SummaryDiatoms are a widespread and ecologically important group of heterokont algae that contribute c. 20% to global productivity. Previous work has shown that regulation of their key Calvin cycle enzymes differs from that of the Plantae, and that in crude extracts, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) can be inhibited by nicotinamide adenine dinucleotide phosphate reduced (NADPH) under oxidizing conditions.The freshwater diatom, Asterionella formosa, was studied using enzyme kinetics, chromatography, surface plasmon resonance, mass spectrometry and sequence analysis to determine the mechanism behind this GAPDH inhibition.GAPDH interacted with ferredoxin-nicotinamide adenine dinucleotide phosphate (NADP) reductase (FNR) from the primary phase of photosynthesis, and the small chloroplast protein, CP12. Sequences of copurified GAPDH and FNR were highly homologous with published sequences. However, the widespread ternary complex among GAPDH, phosphoribulokinase and CP12 was absent. Activity measurements under oxidizing conditions showed that NADPH can inhibit GAPDH-CP12 in the presence of FNR, explaining the earlier observed inhibition within crude extracts.Diatom plastids have a distinctive metabolism, including the lack of the oxidative pentose phosphate pathway, and so cannot produce NADPH in the dark. The observed down-regulation of GAPDH in the dark may allow NADPH to be rerouted towards other reductive processes contributing to their ecological success.

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Regulation of glyceraldehyde-3-phosphate dehydrogenase in the eustigmatophytePseudocharaciopsis ovalisis intermediate between a chlorophyte and a diatom

Cited by 6 publications

References 48 publications

Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii

Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii

Regulation of Carbon Metabolism by Environmental Conditions: A Perspective From Diatoms and Other Chromalveolates

Glyceraldehyde‐3‐phosphate dehydrogenase is regulated by ferredoxin‐NADP reductase in the diatom Asterionella formosa

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