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- Title
Evolutionarily Conserved Iron-Sulfur Protein INDH Is Required for Complex I Assembly and Mitochondrial Translation in Arabidopsis.
- Authors
Wydro, Mateusz M.; Sharma, Pia; Foster, Jonathan M.; Bych, Katrine; Meyer, Etienne H.; Balk, Janneke
- Abstract
The assembly of respiratory complexes is a multistep process, requiring coordinate expression of mitochondrial and nuclear genes and cofactor biosynthesis. We functionally characterized the iron-sulfur protein required for NADH dehydrogenase (INDH) in the model plant Arabidopsis thaliana. An indh knockout mutant lacked complex I but had low levels of a 650-kD assembly intermediate, similar to mutations in the homologous NUBPL (nucleotide binding protein-like) in Homo sapiens. However, heterozygous indh /+ mutants displayed unusual phenotypes during gametogenesis and resembled mutants in mitochondrial translation more than mutants in complex I. Gradually increased expression of INDH in indh knockout plants revealed a significant delay in reassembly of complex I, suggesting an indirect role for INDH in the assembly process. Depletion of INDH protein was associated with decreased 35S-Met labeling of translation products in isolated mitochondria, whereas the steady state levels of several mitochondrial transcripts were increased. Mitochondrially encoded proteins were differentially affected, with near normal levels of cytochrome c oxidase subunit2 and Nad7 but little Nad6 protein in the indh mutant. These data suggest that INDH has a primary role in mitochondrial translation that underlies its role in complex I assembly.
- Subjects
IRON-sulfur proteins; GENETIC translation; CYTOCHROME oxidase; MITOCHONDRIA; NADH dehydrogenase; MUTANT proteins; NAD (Coenzyme)
- Publication
Plant Cell, 2013, Vol 25, Issue 10, p4014
- ISSN
1040-4651
- Publication type
Article
- DOI
10.1105/tpc.113.117283