Details
| Original language | English |
|---|---|
| Pages (from-to) | 1658-1668 |
| Number of pages | 11 |
| Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
| Volume | 1814 |
| Issue number | 12 |
| Publication status | Published - 22 Aug 2011 |
Abstract
Legumes carry out special biochemical functions, e.g. the fixation of molecular nitrogen based on a symbiosis with proteobacteria. At the cellular level, this symbiosis has to be implemented into the energy metabolism of the host cell. To provide a basis for future analyses, we have characterized the protein complement of mitochondria of the model legume Medicago truncatula using two-dimensional isoelectric focussing (IEF) and blue-native (BN)-SDS-PAGE. While the IEF reference map resulted mainly in resolution of those proteins associated with the mitochondrial matrix, the BN proteomic map allowed separation of protein subunits from the respiratory chain protein complexes, which are located in the organelle's inner membrane. The M. truncatula mitochondrial BN reference map revealed some striking similarities to the one from Arabidopsis thaliana but at the same time exhibited also some special features: complex II is of increased abundance and additionally represented by a low molecular mass form not reported for Arabidopsis. Furthermore three highly abundant forms of prohibitin complexes are present in the mitochondrial proteome of M. truncatula. Special features with respect to mitochondrial protein complexes might reflect adaptations of legumes to elevated cellular energy requirements enabling them to develop symbiotic interactions with rhizobial bacteria.
Keywords
- Blue-native (BN), Complex II (succinate dehydrogenase), Medicago truncatula, Mitochondrial prohibitin, Mitochondrial proteome, SDS-PAGE
ASJC Scopus subject areas
- Chemistry(all)
- Analytical Chemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
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In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1814, No. 12, 22.08.2011, p. 1658-1668.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The mitochondrial proteome of the model legume Medicago truncatula
AU - Dubinin, Juri
AU - Braun, Hans Peter
AU - Schmitz, Udo
AU - Colditz, Frank
PY - 2011/8/22
Y1 - 2011/8/22
N2 - Legumes carry out special biochemical functions, e.g. the fixation of molecular nitrogen based on a symbiosis with proteobacteria. At the cellular level, this symbiosis has to be implemented into the energy metabolism of the host cell. To provide a basis for future analyses, we have characterized the protein complement of mitochondria of the model legume Medicago truncatula using two-dimensional isoelectric focussing (IEF) and blue-native (BN)-SDS-PAGE. While the IEF reference map resulted mainly in resolution of those proteins associated with the mitochondrial matrix, the BN proteomic map allowed separation of protein subunits from the respiratory chain protein complexes, which are located in the organelle's inner membrane. The M. truncatula mitochondrial BN reference map revealed some striking similarities to the one from Arabidopsis thaliana but at the same time exhibited also some special features: complex II is of increased abundance and additionally represented by a low molecular mass form not reported for Arabidopsis. Furthermore three highly abundant forms of prohibitin complexes are present in the mitochondrial proteome of M. truncatula. Special features with respect to mitochondrial protein complexes might reflect adaptations of legumes to elevated cellular energy requirements enabling them to develop symbiotic interactions with rhizobial bacteria.
AB - Legumes carry out special biochemical functions, e.g. the fixation of molecular nitrogen based on a symbiosis with proteobacteria. At the cellular level, this symbiosis has to be implemented into the energy metabolism of the host cell. To provide a basis for future analyses, we have characterized the protein complement of mitochondria of the model legume Medicago truncatula using two-dimensional isoelectric focussing (IEF) and blue-native (BN)-SDS-PAGE. While the IEF reference map resulted mainly in resolution of those proteins associated with the mitochondrial matrix, the BN proteomic map allowed separation of protein subunits from the respiratory chain protein complexes, which are located in the organelle's inner membrane. The M. truncatula mitochondrial BN reference map revealed some striking similarities to the one from Arabidopsis thaliana but at the same time exhibited also some special features: complex II is of increased abundance and additionally represented by a low molecular mass form not reported for Arabidopsis. Furthermore three highly abundant forms of prohibitin complexes are present in the mitochondrial proteome of M. truncatula. Special features with respect to mitochondrial protein complexes might reflect adaptations of legumes to elevated cellular energy requirements enabling them to develop symbiotic interactions with rhizobial bacteria.
KW - Blue-native (BN)
KW - Complex II (succinate dehydrogenase)
KW - Medicago truncatula
KW - Mitochondrial prohibitin
KW - Mitochondrial proteome
KW - SDS-PAGE
UR - http://www.scopus.com/inward/record.url?scp=80054761744&partnerID=8YFLogxK
U2 - 10.1016/j.bbapap.2011.08.008
DO - 10.1016/j.bbapap.2011.08.008
M3 - Article
C2 - 21893218
AN - SCOPUS:80054761744
VL - 1814
SP - 1658
EP - 1668
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 12
ER -