Molecular adaptations of NADP-malic enzyme for its function in C4 photosynthesis in grasses

Autor: Martin J. Lercher, Luitgard Nagel-Steger, Alejandro Buschiazzo, Astrid Höppner, Anastasiia Bovdilova, Maria F. Drincovich, Mariana Saigo, Clarisa E. Alvarez, Veronica G. Maurino, Tao Zhang, Christian-Claus Wolff, Felipe Trajtenberg
Přispěvatelé: Universidad Nacional de Rosario [Santa Fe], Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Cluster of Excellence on Plant Sciences (CEPLAS), Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ)-Universität zu Köln = University of Cologne, Molecular and structural microbiology / Microbiología Molecular y Estructural [Montevideo], Institut Pasteur de Montevideo, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Institute of Complex Systems (ICS), Forschungszentrum Jülich GmbH | Centre de recherche de Juliers, Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association, Integrative Microbiology of Zoonotic Agents [Paris and Montevideo] (IMiZA), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut Pasteur [Paris] (IP), This work was funded by grants of the European Union (3to4) to V.G.M. and by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany´s Excellence Strategy (EXC 2048/1, Project ID: 390686111 and EXC 1028, to V.G.M. and M.J.L., European Project: 289582,EC:FP7:KBBE,FP7-KBBE-2011-5,3TO4(2012), Universität zu Köln-Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf]-Max Planck Institute for Plant Breeding Research (MPIPZ), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut Pasteur [Paris]
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Zdroj: Nature Plants
Nature Plants, 2019, 5 (7), pp.755-765. ⟨10.1038/s41477-019-0451-7⟩
Nature plants 5(7), 755-765 (2019). doi:10.1038/s41477-019-0451-7
Nature Plants, Nature Publishing Group, 2019, 5 (7), pp.755-765. ⟨10.1038/s41477-019-0451-7⟩
ISSN: 2055-026X
2055-0278
Popis: In C4 grasses of agronomical interest, malate shuttled into the bundle sheath cells is decarboxylated mainly by nicotinamide adenine dinucleotide phosphate (NADP)-malic enzyme (C4-NADP-ME). The activity of C4-NADP-ME was optimized by natural selection to efficiently deliver CO2 to Rubisco. During its evolution from a plastidic non-photosynthetic NADP-ME, C4-NADP-ME acquired increased catalytic efficiency, tetrameric structure and pH-dependent inhibition by its substrate malate. Here, we identified specific amino acids important for these C4 adaptions based on strict differential conservation of amino acids, combined with solving the crystal structures of maize and sorghum C4-NADP-ME. Site-directed mutagenesis and struc-tural analyses show that Q503, L544 and E339 are involved in catalytic efficiency; E339 confers pH-dependent regulation by malate, F140 is critical for the stabilization of the oligomeric structure and the N-terminal region is involved in tetramerization. Together, the identified molecular adaptations form the basis for the efficient catalysis and regulation of one of the central biochemical steps in C4 metabolism
Databáze: OpenAIRE
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