Corrigendum to: Posttranslational Modification of the NADP-Malic Enzyme Involved in C4 Photosynthesis Modulates the Enzymatic Activity during the Day
| Autor: | David Bickel, Saleh Alseekh, Luitgard Nagel-Steger, Inês M. Luís, Astrid Höppner, Clarisa E. Alvarez, María F. Drincovich, Holger Gohlke, Bruno M. Alexandre, Alisdair R. Fernie, Christina Decker, Anastasiia Bovdilova, Veronica G. Maurino, Isabel A. Abreu |
|---|---|
| Rok vydání: | 2021 |
| Předmět: | |
| Zdroj: | The Plant cell Plant Cell |
| ISSN: | 1532-298X 1040-4651 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|