Posttranslational Modification of the NADP-Malic Enzyme Involved in C4 Photosynthesis Modulates the Enzymatic Activity during the Day. Issue 10 (30th July 2019)
- Record Type:
- Journal Article
- Title:
- Posttranslational Modification of the NADP-Malic Enzyme Involved in C4 Photosynthesis Modulates the Enzymatic Activity during the Day. Issue 10 (30th July 2019)
- Main Title:
- Posttranslational Modification of the NADP-Malic Enzyme Involved in C4 Photosynthesis Modulates the Enzymatic Activity during the Day
- Authors:
- Bovdilova, Anastasiia
Alexandre, Bruno M.
Höppner, Astrid
Luís, Inês Matias
Alvarez, Clarisa E.
Bickel, David
Gohlke, Holger
Decker, Christina
Nagel-Steger, Luitgard
Alseekh, Saleh
Fernie, Alisdair R.
Drincovich, Maria F.
Abreu, Isabel A.
Maurino, Veronica G. - Abstract:
- Abstract : Phosphorylation of maize C4-NADP-malic enzyme at a specific Ser residue decreases the binding affinity to the cofactor, reducing the enzymatic activity during the first hours in the light. Abstract: Evolution of the C4 photosynthetic pathway involved in some cases recruitment of housekeeping proteins through gene duplication and their further neofunctionalization. NADP-malic enzyme (ME), the most widespread C4 decarboxylase, has increased its catalytic efficiency and acquired regulatory properties that allowed it to participate in the C4 pathway. Here, we show that regulation of maize ( Zea mays ) C4 -NADP-ME activity is much more elaborate than previously thought. Using mass spectrometry, we identified phosphorylation of the Ser419 residue of C4 -NADP-ME in protein extracts of maize leaves. The phosphorylation event increases in the light, with a peak at Zeitgeber time 2. Phosphorylation of ZmC4 -NADP-ME drastically decreases its activity as shown by the low residual activity of the recombinant phosphomimetic mutant. Analysis of the crystal structure of C4 -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 ZmC4 -NADP-ME at Ser419 during the first hours in the light is a cellular mechanism that fine tunes theAbstract : Phosphorylation of maize C4-NADP-malic enzyme at a specific Ser residue decreases the binding affinity to the cofactor, reducing the enzymatic activity during the first hours in the light. Abstract: Evolution of the C4 photosynthetic pathway involved in some cases recruitment of housekeeping proteins through gene duplication and their further neofunctionalization. NADP-malic enzyme (ME), the most widespread C4 decarboxylase, has increased its catalytic efficiency and acquired regulatory properties that allowed it to participate in the C4 pathway. Here, we show that regulation of maize ( Zea mays ) C4 -NADP-ME activity is much more elaborate than previously thought. Using mass spectrometry, we identified phosphorylation of the Ser419 residue of C4 -NADP-ME in protein extracts of maize leaves. The phosphorylation event increases in the light, with a peak at Zeitgeber time 2. Phosphorylation of ZmC4 -NADP-ME drastically decreases its activity as shown by the low residual activity of the recombinant phosphomimetic mutant. Analysis of the crystal structure of C4 -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 ZmC4 -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 CO2 fixation rate, probably to avoid CO2 leakiness from bundle sheath cells. … (more)
- Is Part Of:
- The Plant Cell. Volume 31:Issue 10(2019)
- Journal:
- The Plant Cell
- Issue:
- Volume 31:Issue 10(2019)
- Issue Display:
- Volume 31, Issue 10 (2019)
- Year:
- 2019
- Volume:
- 31
- Issue:
- 10
- Issue Sort Value:
- 2019-0031-0010-0000
- Page Start:
- 2525
- Page End:
- 2539
- Publication Date:
- 2019-07-30
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.19.00406 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 22057.xml