Pyrroline-5-carboxylate dehydrogenase is a key player in nitrogen metabolism in maturing seeds of Arabidopsis thaliana

Authored by

Corentin Dourmap, Sébastien Baud, Holger Eubel, Nils Rugen, Émilie Crilat, Solenne Beradocco, Nathalie Marnet, Gilles Clément, Guillaume Tcherkez, Séverine Planchais, Cécile Cabassa, Sandrine Lebreton, Marianne Bordenave-Jacquemin, Régis Maldiney, Pierre Carol, Hans-Peter Braun, Céline Masclaux-Daubresse, Alain Bouchereau, Arnould Savouré, Anne Guivarc’h

Abstract

Proline is a multifaceted amino acid in plants involved in both stress responses and development. Recent studies have shown that knockout mutants lacking pyrroline-5-carboxylate dehydrogenase (P5CDH), the enzyme responsible for the second step of proline catabolism, have impaired nitrogen remobilization and carbon allocation to seeds. Here, we demonstrate that seed development is also significantly impaired in p5cdh mutants, particularly during the transition between embryogenesis and maturation. Specifically, the p5cdh mutation leads to an arrest in embryo elongation and a reprogramming of seed metabolism during maturation, resulting in reduced accumulation of storage compounds and compromised acquisition of dehydration tolerance. These effects are further exacerbated under high-nitrate conditions. Together, our findings highlight a crucial role for proline catabolism in supporting the ability of maturing embryos to utilize glutamine as a nitrogen source, particularly in response to nitrogen availability.

Details

Organisation(s)
Section Plant Molecular Biology and Plant Proteomics
External Organisation(s)
Sorbonne Université
Université Paris-Saclay
Universite de Rennes 1
University of Angers
Australian National University
Type
Article
Journal
Journal of Experimental Botany
Volume
77
Pages
1827-1843
No. of pages
17
ISSN
0022-0957
Publication date
17.03.2026
Publication status
Published
Peer reviewed
Yes
ASJC Scopus subject areas
Physiology, Plant Science
Electronic version(s)
https://doi.org/10.1093/jxb/eraf542 (Access: Closed )