Journal
BIOCHEMICAL JOURNAL
Volume 473, Issue -, Pages 2623-2634Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BCJ20160314
Keywords
Arabidopsis thaliana; electron transfer chain; mitochondria; proline; proline dehydrogenase (ProDH)
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Funding
- UPMC
- Leibniz University Hannover
- Deutsche Akademische Austauschdienst [55903318]
- Ministry of Foreign Affairs [28404PH]
- Tunisian-French UTIQUE network [13G0929]
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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.
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