Details
| Original language | English |
|---|---|
| Pages (from-to) | 2794-2804 |
| Number of pages | 11 |
| Journal | FEBS Journal |
| Volume | 281 |
| Issue number | 12 |
| Early online date | 14 May 2014 |
| Publication status | Published - 18 Jun 2014 |
Abstract
Proline has multiple functions in plants. Besides being a building block for protein biosynthesis proline plays a central role in the plant stress response and in further cellular processes. Here, we report an analysis on the integration of proline dehydrogenase (ProDH) into mitochondrial metabolism in Arabidopsis thaliana. An experimental system to induce ProDH activity was established using cell cultures. Induction of ProDH was measured by novel photometric activity assays and by a ProDH in gel activity assay. Effects of increased ProDH activity on other mitochondrial enzymes were systematically investigated. Activities of the protein complexes of the respiratory chain were not significantly altered. In contrast, some mitochondrial dehydrogenases had markedly changed activities. Activity of glutamate dehydrogenase substantially increased, indicating upregulation of the entire proline catabolic pathway, which was confirmed by co-expression analyses of the corresponding genes. Furthermore, activity of d-lactate dehydrogenase was increased. d-lactate was identified to be a competitive inhibitor of ProDH in plants. We suggest that induction of d-lactate dehydrogenase activity allows rapid upregulation of ProDH activity during the short-term stress response in plants.
Keywords
- At3g30775, dehydrogenase, enzyme inhibitor, mitochondria, plant, proline, proline dehydrogenase (ProDH), stress response
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS Journal, Vol. 281, No. 12, 18.06.2014, p. 2794-2804.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Biochemical characterization of proline dehydrogenase in Arabidopsis mitochondria
AU - Schertl, Peter
AU - Cabassa, Cécile
AU - Saadallah, Kaouthar
AU - Bordenave, Marianne
AU - Savouré, Arnould
AU - Braun, Hans Peter
PY - 2014/6/18
Y1 - 2014/6/18
N2 - Proline has multiple functions in plants. Besides being a building block for protein biosynthesis proline plays a central role in the plant stress response and in further cellular processes. Here, we report an analysis on the integration of proline dehydrogenase (ProDH) into mitochondrial metabolism in Arabidopsis thaliana. An experimental system to induce ProDH activity was established using cell cultures. Induction of ProDH was measured by novel photometric activity assays and by a ProDH in gel activity assay. Effects of increased ProDH activity on other mitochondrial enzymes were systematically investigated. Activities of the protein complexes of the respiratory chain were not significantly altered. In contrast, some mitochondrial dehydrogenases had markedly changed activities. Activity of glutamate dehydrogenase substantially increased, indicating upregulation of the entire proline catabolic pathway, which was confirmed by co-expression analyses of the corresponding genes. Furthermore, activity of d-lactate dehydrogenase was increased. d-lactate was identified to be a competitive inhibitor of ProDH in plants. We suggest that induction of d-lactate dehydrogenase activity allows rapid upregulation of ProDH activity during the short-term stress response in plants.
AB - Proline has multiple functions in plants. Besides being a building block for protein biosynthesis proline plays a central role in the plant stress response and in further cellular processes. Here, we report an analysis on the integration of proline dehydrogenase (ProDH) into mitochondrial metabolism in Arabidopsis thaliana. An experimental system to induce ProDH activity was established using cell cultures. Induction of ProDH was measured by novel photometric activity assays and by a ProDH in gel activity assay. Effects of increased ProDH activity on other mitochondrial enzymes were systematically investigated. Activities of the protein complexes of the respiratory chain were not significantly altered. In contrast, some mitochondrial dehydrogenases had markedly changed activities. Activity of glutamate dehydrogenase substantially increased, indicating upregulation of the entire proline catabolic pathway, which was confirmed by co-expression analyses of the corresponding genes. Furthermore, activity of d-lactate dehydrogenase was increased. d-lactate was identified to be a competitive inhibitor of ProDH in plants. We suggest that induction of d-lactate dehydrogenase activity allows rapid upregulation of ProDH activity during the short-term stress response in plants.
KW - At3g30775
KW - dehydrogenase
KW - enzyme inhibitor
KW - mitochondria
KW - plant
KW - proline
KW - proline dehydrogenase (ProDH)
KW - stress response
UR - http://www.scopus.com/inward/record.url?scp=84902658522&partnerID=8YFLogxK
U2 - 10.1111/febs.12821
DO - 10.1111/febs.12821
M3 - Article
C2 - 24751239
AN - SCOPUS:84902658522
VL - 281
SP - 2794
EP - 2804
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 12
ER -