Posttranslational Modification of the NADP-Malic Enzyme Involved in C 4 Photosynthesis Modulates the Enzymatic Activity during the Day.

Autor: Bovdilova A; Institute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich Heine University Düsseldorf, Universitätsstraße 1, and Cluster of Excellence on Plant Sciences (CEPLAS), 40225 Düsseldorf, Germany., Alexandre BM; Instituto de Biologia Experimental e Tecnológica, Avenida da República, Quinta do Marquês, 2780-157 Oeiras, Portugal.; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, 2780-157 Oeiras, Portugal., Höppner A; Center for Structural Studies (CSS), Heinrich Heine University Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany., Luís IM; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, 2780-157 Oeiras, Portugal., Alvarez CE; Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, University of Rosario, Suipacha 570, 2000 Rosario, Argentina., Bickel D; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany., Gohlke H; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany.; John von Neumann Institute for Computing (NIC), Jülich Supercomputing Centre (JSC) and Institute for Complex Systems-Structural Biochemistry (ICS 6), Forschungszentrum Jülich GmbH, 52425 Jülich, Germany., Decker C; Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany.; Institute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany., Nagel-Steger L; Institut für Physikalische Biologie, Heinrich Heine University Düsseldorf, Universitätsstraße 1, 40225 Düsseldorf, Germany.; Institute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany., Alseekh S; Max-Planck-Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam-Golm, Germany.; Center for Systems Biology and Biotechnology, 4000 Plovdiv, Bulgaria., Fernie AR; Max-Planck-Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam-Golm, Germany., Drincovich MF; Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, University of Rosario, Suipacha 570, 2000 Rosario, Argentina., Abreu IA; Instituto de Biologia Experimental e Tecnológica, Avenida da República, Quinta do Marquês, 2780-157 Oeiras, Portugal.; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Avenida da República, 2780-157 Oeiras, Portugal., Maurino VG; Institute of Developmental and Molecular Biology of Plants, Plant Molecular Physiology and Biotechnology Group, Heinrich Heine University Düsseldorf, Universitätsstraße 1, and Cluster of Excellence on Plant Sciences (CEPLAS), 40225 Düsseldorf, Germany veronica.maurino@uni-duesseldorf.de.
Jazyk: angličtina
Zdroj: The Plant cell [Plant Cell] 2019 Oct; Vol. 31 (10), pp. 2525-2539. Date of Electronic Publication: 2019 Jul 30.
DOI: 10.1105/tpc.19.00406
Abstrakt: Evolution of the C 4 photosynthetic pathway involved in some cases recruitment of housekeeping proteins through gene duplication and their further neofunctionalization. NADP-malic enzyme (ME), the most widespread C 4 decarboxylase, has increased its catalytic efficiency and acquired regulatory properties that allowed it to participate in the C 4 pathway. Here, we show that regulation of maize ( Zea mays ) C 4 -NADP-ME activity is much more elaborate than previously thought. Using mass spectrometry, we identified phosphorylation of the Ser419 residue of C 4 -NADP-ME in protein extracts of maize leaves. The phosphorylation event increases in the light, with a peak at Zeitgeber time 2. Phosphorylation of ZmC 4 -NADP-ME drastically decreases its activity as shown by the low residual activity of the recombinant phosphomimetic mutant. Analysis of the crystal structure of C 4 -NADP-ME indicated that Ser419 is involved in the binding of NADP at the active site. Molecular dynamics simulations and effective binding energy computations indicate a less favorable binding of the cofactor NADP in the phosphomimetic and the phosphorylated variants. We propose that phosphorylation of ZmC 4 -NADP-ME at Ser419 during the first hours in the light is a cellular mechanism that fine tunes the enzymatic activity to coordinate the carbon concentration mechanism with the CO 2 fixation rate, probably to avoid CO 2 leakiness from bundle sheath cells.
(© 2019 American Society of Plant Biologists. All rights reserved.)
Databáze: MEDLINE
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