Glyceraldehyde-3-phosphate dehydrogenase is regulated by ferredoxin-NADP reductase in the diatom Asterionella formosa. 2014

Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
Aix-Marseille Université CNRS, BIP UMR 7281, 31 Chemin Joseph Aiguier, 13402, Marseille Cedex 20, France.

Diatoms 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.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009249 NADP Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed) Coenzyme II,Nicotinamide-Adenine Dinucleotide Phosphate,Triphosphopyridine Nucleotide,NADPH,Dinucleotide Phosphate, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide Phosphate,Nucleotide, Triphosphopyridine,Phosphate, Nicotinamide-Adenine Dinucleotide
D010802 Phylogeny The relationships of groups of organisms as reflected by their genetic makeup. Community Phylogenetics,Molecular Phylogenetics,Phylogenetic Analyses,Phylogenetic Analysis,Phylogenetic Clustering,Phylogenetic Comparative Analysis,Phylogenetic Comparative Methods,Phylogenetic Distance,Phylogenetic Generalized Least Squares,Phylogenetic Groups,Phylogenetic Incongruence,Phylogenetic Inference,Phylogenetic Networks,Phylogenetic Reconstruction,Phylogenetic Relatedness,Phylogenetic Relationships,Phylogenetic Signal,Phylogenetic Structure,Phylogenetic Tree,Phylogenetic Trees,Phylogenomics,Analyse, Phylogenetic,Analysis, Phylogenetic,Analysis, Phylogenetic Comparative,Clustering, Phylogenetic,Community Phylogenetic,Comparative Analysis, Phylogenetic,Comparative Method, Phylogenetic,Distance, Phylogenetic,Group, Phylogenetic,Incongruence, Phylogenetic,Inference, Phylogenetic,Method, Phylogenetic Comparative,Molecular Phylogenetic,Network, Phylogenetic,Phylogenetic Analyse,Phylogenetic Clusterings,Phylogenetic Comparative Analyses,Phylogenetic Comparative Method,Phylogenetic Distances,Phylogenetic Group,Phylogenetic Incongruences,Phylogenetic Inferences,Phylogenetic Network,Phylogenetic Reconstructions,Phylogenetic Relatednesses,Phylogenetic Relationship,Phylogenetic Signals,Phylogenetic Structures,Phylogenetic, Community,Phylogenetic, Molecular,Phylogenies,Phylogenomic,Reconstruction, Phylogenetic,Relatedness, Phylogenetic,Relationship, Phylogenetic,Signal, Phylogenetic,Structure, Phylogenetic,Tree, Phylogenetic
D003624 Darkness The absence of light. Darknesses
D005287 Ferredoxin-NADP Reductase An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4. Adrenodoxin Reductase,Iron-Sulfur Protein Reductase,NADPH-Ferredoxin Reductase,Ferredoxin NADP Reductase,Iron Sulfur Protein Reductase,NADPH Ferredoxin Reductase,Protein Reductase, Iron-Sulfur,Reductase, Adrenodoxin,Reductase, Ferredoxin-NADP,Reductase, Iron-Sulfur Protein,Reductase, NADPH-Ferredoxin
D005987 Glyceraldehyde-3-Phosphate Dehydrogenases Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD. GAPD,Glyceraldehyde-3-Phosphate Dehydrogenase,Glyceraldehydephosphate Dehydrogenase,Phosphoglyceraldehyde Dehydrogenase,Triosephosphate Dehydrogenase,Dehydrogenase, Glyceraldehyde-3-Phosphate,Dehydrogenase, Glyceraldehydephosphate,Dehydrogenase, Phosphoglyceraldehyde,Dehydrogenase, Triosephosphate,Dehydrogenases, Glyceraldehyde-3-Phosphate,Glyceraldehyde 3 Phosphate Dehydrogenase
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D017377 Diatoms The common name for the phylum of microscopic unicellular STRAMENOPILES. Most are aquatic, being found in fresh, brackish, and salt water. Diatoms are noted for the symmetry and sculpturing of their siliceous cell walls. They account for 40% of PHYTOPLANKTON, but not all diatoms are planktonic. Bacillariophyta,Bacillariophytas,Diatom
D020349 Surface Plasmon Resonance A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding. Plasmon Resonance, Surface,Plasmon Resonances, Surface,Resonance, Surface Plasmon,Resonances, Surface Plasmon,Surface Plasmon Resonances

Related Publications

Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
December 2008, Journal of phycology,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
January 2008, Journal of structural biology,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
April 1978, Plant physiology,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
June 2015, Molecular ecology,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
October 2010, The international journal of biochemistry & cell biology,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
May 1990, Archives of biochemistry and biophysics,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
February 2017, Mitochondrial DNA. Part B, Resources,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
January 1998, The Journal of biological chemistry,
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
September 2001, Microbiology (Reading, England),
Malika Mekhalfi, and Carine Puppo, and Luisana Avilan, and Régine Lebrun, and Pascal Mansuelle, and Stephen C Maberly, and Brigitte Gontero
January 1973, Biochimica et biophysica acta,
Copied contents to your clipboard!