Details
| Original language | English |
|---|---|
| Pages (from-to) | 194-207 |
| Number of pages | 14 |
| Journal | New Phytologist |
| Volume | 211 |
| Issue number | 1 |
| Publication status | Published - 31 May 2016 |
Abstract
Complex I of the mitochondrial electron transport chain (mETC) in plants contains an extra domain that is made up from proteins homologous to prokaryotic gamma-carbonic anhydrases (γCA). This domain has been suggested to participate in complex I assembly or to support transport of mitochondrial CO2 to the chloroplast. Here, we generated mutants lacking CA1 and CA2 - two out of three CA proteins in Arabidopsis thaliana. Double mutants were characterized at the developmental and physiological levels. Furthermore, the composition and activity of the mETC were determined, and mutated CA versions were used for complementation assays. Embryo development of double mutants was strongly delayed and seed development stopped before maturation. Mutant plants could only be rescued on sucrose media, showed severe stress symptoms and never produced viable seeds. By contrast, callus cultures were only slightly affected in growth. Complex I was undetectable in the double mutants, but complex II and complex IV were upregulated concomitant with increased oxygen consumption in mitochondrial respiration. Ectopic expression of inactive CA variants was sufficient to complement the mutant phenotype. Data indicate that CA proteins are structurally required for complex I assembly and that reproductive development is dependent on the presence of complex I.
Keywords
- NADH, Arabidopsis thaliana, Carbonic anhydrase (γCA), Complex I, Mitochondrial metabolism, Respiratory chain, Ubiquinone oxidoreductase
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Physiology
- Agricultural and Biological Sciences(all)
- Plant Science
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In: New Phytologist, Vol. 211, No. 1, 31.05.2016, p. 194-207.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Mitochondrial gamma carbonic anhydrases are required for complex I assembly and plant reproductive development
AU - Fromm, Steffanie
AU - Braun, Hans Peter
AU - Peterhansel, Christoph
N1 - This work was supported by the Deutsche Forschungsgemeinschaft (DFG), Forschergruppe 1186 (grant Br1829/10-2). We gratefully acknowledge Professor Dr Traud Winkelmann for her support with DIC microscopy and the embryo rescue technique and Dr Etienne Meyer for providing the ndufs4 mutant.
PY - 2016/5/31
Y1 - 2016/5/31
N2 - Complex I of the mitochondrial electron transport chain (mETC) in plants contains an extra domain that is made up from proteins homologous to prokaryotic gamma-carbonic anhydrases (γCA). This domain has been suggested to participate in complex I assembly or to support transport of mitochondrial CO2 to the chloroplast. Here, we generated mutants lacking CA1 and CA2 - two out of three CA proteins in Arabidopsis thaliana. Double mutants were characterized at the developmental and physiological levels. Furthermore, the composition and activity of the mETC were determined, and mutated CA versions were used for complementation assays. Embryo development of double mutants was strongly delayed and seed development stopped before maturation. Mutant plants could only be rescued on sucrose media, showed severe stress symptoms and never produced viable seeds. By contrast, callus cultures were only slightly affected in growth. Complex I was undetectable in the double mutants, but complex II and complex IV were upregulated concomitant with increased oxygen consumption in mitochondrial respiration. Ectopic expression of inactive CA variants was sufficient to complement the mutant phenotype. Data indicate that CA proteins are structurally required for complex I assembly and that reproductive development is dependent on the presence of complex I.
AB - Complex I of the mitochondrial electron transport chain (mETC) in plants contains an extra domain that is made up from proteins homologous to prokaryotic gamma-carbonic anhydrases (γCA). This domain has been suggested to participate in complex I assembly or to support transport of mitochondrial CO2 to the chloroplast. Here, we generated mutants lacking CA1 and CA2 - two out of three CA proteins in Arabidopsis thaliana. Double mutants were characterized at the developmental and physiological levels. Furthermore, the composition and activity of the mETC were determined, and mutated CA versions were used for complementation assays. Embryo development of double mutants was strongly delayed and seed development stopped before maturation. Mutant plants could only be rescued on sucrose media, showed severe stress symptoms and never produced viable seeds. By contrast, callus cultures were only slightly affected in growth. Complex I was undetectable in the double mutants, but complex II and complex IV were upregulated concomitant with increased oxygen consumption in mitochondrial respiration. Ectopic expression of inactive CA variants was sufficient to complement the mutant phenotype. Data indicate that CA proteins are structurally required for complex I assembly and that reproductive development is dependent on the presence of complex I.
KW - NADH
KW - Arabidopsis thaliana
KW - Carbonic anhydrase (γCA)
KW - Complex I
KW - Mitochondrial metabolism
KW - Respiratory chain
KW - Ubiquinone oxidoreductase
UR - http://www.scopus.com/inward/record.url?scp=84959122278&partnerID=8YFLogxK
U2 - 10.1111/nph.13886
DO - 10.1111/nph.13886
M3 - Article
C2 - 26889912
AN - SCOPUS:84959122278
VL - 211
SP - 194
EP - 207
JO - New Phytologist
JF - New Phytologist
SN - 0028-646X
IS - 1
ER -