Chloroplast FBPase and SBPase are thioredoxin-linked enzymes with similar architecture but different evolutionary histories
| Autor: | Arnaud Hecker, Desirée D. Gütle, Thomas Roret, Stefanie J. Müller, Oliver Einsle, Jean-Pierre Jacquot, Stéphane D. Lemaire, Tiphaine Dhalleine, Bob B. Buchanan, Ralf Reski, Jérémy Couturier |
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| Přispěvatelé: | Plant Biotechnology, Faculty of Biology, University of Freiburg, Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Spemann Graduate School of Biology and Medicine (SGBM), Rheinische Friedrich-Wilhelms-Universität Bonn, Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes (LBMCE), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Lawrence Berkeley National Laboratory [Berkeley] (LBNL), BIOSS − Centre for Biological Signalling Studies, Freiburg Institute for Advanced Studies, Institut für Biochemie und Molekularbiologie, Freiburg, Albert-Ludwigs-Universität Freiburg, ANR (ANR-11-LABX-0002-01, ANR-11-LABX-0011 LABEX DYNAMO), Excellence Initiative of the German Federal and State Governments (EXC294), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
0301 basic medicine Evolution 1.1 Normal biological development and functioning [SDV]Life Sciences [q-bio] Fructose 1 6-bisphosphatase Calvin–Benson cycle thiol-disulfide exchange Physcomitrella patens 01 natural sciences sedoheptulose-1 Evolution Molecular redox regulation 03 medical and health sciences chemistry.chemical_compound Chloroplast Proteins Thioredoxins Underpinning research 6-bisphosphatase Light-independent reactions Ferredoxin chemistry.chemical_classification Multidisciplinary biology Calvin-Benson cycle Molecular Biological Sciences biology.organism_classification Bryopsida Phosphoric Monoester Hydrolases Fructose-Bisphosphatase Chloroplast 030104 developmental biology Sedoheptulose Enzyme Biochemistry chemistry biology.protein 7-bisphosphatase thiol–disulfide exchange fructose-1 Thioredoxin 010606 plant biology & botany |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2016, 113 (24), pp.6779-6784. ⟨10.1073/pnas.1606241113⟩ Proceedings of the National Academy of Sciences of the United States of America, 2016, 113 (24), pp.6779-6784. ⟨10.1073/pnas.1606241113⟩ Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 24 |
| ISSN: | 0027-8424 1091-6490 |
| DOI: | 10.1073/pnas.1606241113⟩ |
| Popis: | International audience; The Calvin-Benson cycle of carbon dioxide fixation in chloroplasts is controlled by light-dependent redox reactions that target specific enzymes. Of the regulatorymembers of the cycle, our knowledge of sedoheptulose-1,7-bisphosphatase (SBPase) is particularly scanty, despite growing evidence for its importance and link to plant productivity. To help fill this gap, we have purified, crystallized, and characterized the recombinant form of the enzyme together with the better studied fructose-1,6-bisphosphatase (FBPase), in both cases from the moss Physcomitrella patens (Pp). Overall, the moss enzymes resembled their counterparts from seed plants, including oligomeric organization-PpSBPase is a dimer, and PpFBPase is a tetramer. The two phosphatases showed striking structural homology to each other, differing primarily in their solvent-exposed surface areas in a manner accounting for their specificity for seven-carbon (sedoheptulose) and six-carbon (fructose) sugar bisphosphate substrates. The two enzymes had a similar redox potential for their regulatory redoxactive disulfides (-310 mV for PpSBPase vs. -290 mV for PpFBPase), requirement for Mg2+ and thioredoxin (TRX) specificity (TRX f > TRX m). Previously known to differ in the position and sequence of their regulatory cysteines, the enzymes unexpectedly showed unique evolutionary histories. The FBPase gene originated in bacteria in conjunction with the endosymbiotic event giving rise to mitochondria, whereas SBPase arose from an archaeal gene resident in the eukaryotic host. These findings raise the question of how enzymes with such different evolutionary origins achieved structural similarity and adapted to control by the same light-dependent photosynthetic mechanism-namely ferredoxin, ferredoxin-thioredoxin reductase, and thioredoxin. |
| Databáze: | OpenAIRE |
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