Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 2623-2634 |
| Seitenumfang | 12 |
| Fachzeitschrift | Biochemical Journal |
| Jahrgang | 473 |
| Ausgabenummer | 17 |
| Frühes Online-Datum | 30 Aug. 2016 |
| Publikationsstatus | Veröffentlicht - Sept. 2016 |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Biochemical Journal, Jahrgang 473, Nr. 17, 09.2016, S. 2623-2634.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Proteomic and functional analysis of proline dehydrogenase 1 link proline catabolism to mitochondrial electron transport in Arabidopsis thaliana
AU - Cabassa-Hourton, Ćecile
AU - Schertl, Peter
AU - Marianne, Bordenave Jacquemin
AU - Saadallah, Kaouthar
AU - Guivarc'h, Anne
AU - Lebreton, Sandrine
AU - Planchais, Śeverine
AU - Klodmann, Jennifer
AU - Eubel, Holger
AU - Crilat, Emilie
AU - Lefebvre-De Vos, Delphine
AU - Ghelis, Thanos
AU - Richard, Luc
AU - Abdelly, Chedly
AU - Carol, Pierre
AU - Braun, Hans Peter
AU - Savouŕe, Arnould
PY - 2016/9
Y1 - 2016/9
N2 - 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.
AB - 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.
KW - Arabidopsis thaliana
KW - Electron transfer chain
KW - Mitochondria
KW - Proline
KW - Proline dehydrogenase (PRODH)
UR - http://www.scopus.com/inward/record.url?scp=85009382377&partnerID=8YFLogxK
U2 - 10.1042/bcj20160314
DO - 10.1042/bcj20160314
M3 - Article
C2 - 27303048
AN - SCOPUS:85009382377
VL - 473
SP - 2623
EP - 2634
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 17
ER -