Details
| Original language | English |
|---|---|
| Pages (from-to) | 831-844 |
| Number of pages | 14 |
| Journal | Plant Journal |
| Volume | 83 |
| Issue number | 5 |
| Publication status | Published - 3 Jul 2015 |
Abstract
The NADH-ubiquinone oxidoreductase complex (complex I) (EC 1.6.5.3) is the main entrance site of electrons into the respiratory chain. In a variety of eukaryotic organisms, except animals and fungi (Opisthokonta), it contains an extra domain comprising trimers of putative γ-carbonic anhydrases, named the CA domain, which has been proposed to be essential for assembly of complex I. However, its physiological role in plants is not fully understood. Here, we report that Arabidopsis mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Moreover, under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions. Taken together, these results suggest that the CA domain of plant complex I contributes to sustaining efficient photosynthesis under ambient (photorespiratory) conditions. Significance Statement Photorespiration is thought to be an inevitable metabolism derived from the oxygenation activity of Rubisco which produces 2-phosphoglycolate. This pathway allows recycling of a percentage of carbon in plants. In this work we present experimental evidence that the CA domain of the mitochondrial NADH dehydrogenase complex is relevant for the photorespiratory pathway and thus contributes to sustain photosynthesis.
Keywords
- Arabidopsis thaliana, carbon recycling, mitochondria, photorespiration, γ-carbonic anhydrases
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Agricultural and Biological Sciences(all)
- Plant Science
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Plant Journal, Vol. 83, No. 5, 03.07.2015, p. 831-844.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Functional characterization of mutants affected in the carbonic anhydrase domain of the respiratory complex I in Arabidopsis thaliana
AU - Soto, Débora
AU - Cõrdoba, Juan Pablo
AU - Villarreal, Fernando
AU - Bartoli, Carlos
AU - Schmitz, Jessica
AU - Maurino, Veronica G.
AU - Braun, Hans Peter
AU - Pagnussat, Gabriela C.
AU - Zabaleta, Eduardo
PY - 2015/7/3
Y1 - 2015/7/3
N2 - The NADH-ubiquinone oxidoreductase complex (complex I) (EC 1.6.5.3) is the main entrance site of electrons into the respiratory chain. In a variety of eukaryotic organisms, except animals and fungi (Opisthokonta), it contains an extra domain comprising trimers of putative γ-carbonic anhydrases, named the CA domain, which has been proposed to be essential for assembly of complex I. However, its physiological role in plants is not fully understood. Here, we report that Arabidopsis mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Moreover, under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions. Taken together, these results suggest that the CA domain of plant complex I contributes to sustaining efficient photosynthesis under ambient (photorespiratory) conditions. Significance Statement Photorespiration is thought to be an inevitable metabolism derived from the oxygenation activity of Rubisco which produces 2-phosphoglycolate. This pathway allows recycling of a percentage of carbon in plants. In this work we present experimental evidence that the CA domain of the mitochondrial NADH dehydrogenase complex is relevant for the photorespiratory pathway and thus contributes to sustain photosynthesis.
AB - The NADH-ubiquinone oxidoreductase complex (complex I) (EC 1.6.5.3) is the main entrance site of electrons into the respiratory chain. In a variety of eukaryotic organisms, except animals and fungi (Opisthokonta), it contains an extra domain comprising trimers of putative γ-carbonic anhydrases, named the CA domain, which has been proposed to be essential for assembly of complex I. However, its physiological role in plants is not fully understood. Here, we report that Arabidopsis mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Moreover, under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions. Taken together, these results suggest that the CA domain of plant complex I contributes to sustaining efficient photosynthesis under ambient (photorespiratory) conditions. Significance Statement Photorespiration is thought to be an inevitable metabolism derived from the oxygenation activity of Rubisco which produces 2-phosphoglycolate. This pathway allows recycling of a percentage of carbon in plants. In this work we present experimental evidence that the CA domain of the mitochondrial NADH dehydrogenase complex is relevant for the photorespiratory pathway and thus contributes to sustain photosynthesis.
KW - Arabidopsis thaliana
KW - carbon recycling
KW - mitochondria
KW - photorespiration
KW - γ-carbonic anhydrases
UR - http://www.scopus.com/inward/record.url?scp=84940437367&partnerID=8YFLogxK
U2 - 10.1111/tpj.12930
DO - 10.1111/tpj.12930
M3 - Article
C2 - 26148112
AN - SCOPUS:84940437367
VL - 83
SP - 831
EP - 844
JO - Plant Journal
JF - Plant Journal
SN - 0960-7412
IS - 5
ER -