Proteomic and functional analysis of proline dehydrogenase 1 link proline catabolism to mitochondrial electron transport in Arabidopsis thaliana

authored by

Ćecile Cabassa-Hourton, Peter Schertl, Bordenave Jacquemin Marianne, Kaouthar Saadallah, Anne Guivarc'h, Sandrine Lebreton, Śeverine Planchais, Jennifer Klodmann, Holger Eubel, Emilie Crilat, Delphine Lefebvre-De Vos, Thanos Ghelis, Luc Richard, Chedly Abdelly, Pierre Carol, Hans Peter Braun, Arnould Savouŕe

Abstract

Proline accumulates in many plant species in response to environmental stresses. Upon relief from stress, proline is rapidly oxidized in mitochondria by proline dehydrogenase (ProDH) and then by pyrroline-5-carboxylate dehydrogenase (P5CDH). Two ProDH genes have been identified in the genome of the model plant Arabidopsis thaliana. To gain a better understanding of ProDH1 functions in mitochondria, proteomic analysis was performed. ProDH1 polypeptides were identified in Arabidopsis mitochondria by immunoblotting gels after 2D blue native (BN)- SDS/PAGE, probing them with an anti-ProDH antibody and analysing protein spots by MS. The 2D gels showed that ProDH1 forms part of a low-molecular-mass (70-140 kDa) complex in the mitochondrial membrane. To evaluate the contribution of each isoform to proline oxidation, mitochondria were isolated from wild-Type (WT) and prodh1, prodh2, prodh1prodh2 and p5cdh mutants. ProDH activity was high for genotypes in which ProDH, most likely ProDH1,was strongly induced by proline. Respiratory measurements indicate that ProDH1 has a role in oxidizing excess proline and transferring electrons to the respiratory chain.

Organisation(s)

Institute of Plant Genetics
Section Plant Molecular Biology and Plant Proteomics

External Organisation(s)

Center of Biotechnology of Borj Cedria (CBBC)

Type

Article

Journal

Biochemical Journal

Volume

473

Pages

2623-2634

No. of pages

12

ISSN

0264-6021

Publication date

30.08.2016

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Biochemistry, Molecular Biology, Cell Biology

Electronic version(s)

https://doi.org/10.1042/bcj20160314 (Access: Closed)