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

verfasst von

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.

Organisationseinheit(en)

Institut für Pflanzengenetik
Abteilung Pflanzenmolekularbiologie und Pflanzenproteomik

Externe Organisation(en)

Centre de Biotechnologie de Borj Cédria (CBBC)

Typ

Artikel

Journal

Biochemical Journal

Band

473

Seiten

2623-2634

Anzahl der Seiten

12

ISSN

0264-6021

Publikationsdatum

09.2016

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Biochemie, Molekularbiologie, Zellbiologie

Elektronische Version(en)

https://doi.org/10.1042/bcj20160314 (Zugang: Geschlossen)