ArticleThe Plant cell2013
The evolutionarily conserved iron-sulfur protein INDH is required for complex I assembly and mitochondrial translation in Arabidopsis [corrected].
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 68 citations in OpenAlex.
- Article
- Functional Relationships of Two NFU Proteins in Maintaining the Abundances of Mitochondrial Iron-Sulfur Proteins.Plant direct · 2025Article
- The complex I subunit B22 contains a LYR domain that is crucial for an interaction with the mitochondrial acyl carrier protein SDAP1.The Plant journal : for cell and molecular biology · 2025Article
- Aging-induced mitochondrial dysfunction: two distinct populations of mitochondria versus a combined population.American journal of physiology. Heart and circulatory physiology · 2024Article
- The biogenesis and regulation of the plant oxidative phosphorylation system.Plant physiology · 2023Review
- Protein lipoylation in mitochondria requires Fe-S cluster assembly factors NFU4 and NFU5.Plant physiology · 2022Article
- Maturation and Assembly of Iron-Sulfur Cluster-Containing Subunits in the Mitochondrial Complex I From Plants.Frontiers in plant science · 2022Review
- Article
- [4Fe-4S] cluster trafficking mediated byThe Journal of biological chemistry · 2020Article
- Article
- Mitochondrial Pentatricopeptide Repeat Protein, EMB2794, Plays a Pivotal Role in NADH Dehydrogenase Subunit nad2 mRNA Maturation in Arabidopsis thaliana.Plant & cell physiology · 2020Article
- Article
- Pathogenic variants in NUBPL result in failure to assemble the matrix arm of complex I and cause a complex leukoencephalopathy with thalamic involvement.Molecular genetics and metabolism · 2020Article
- A Mitochondrial LYR Protein Is Required for Complex I Assembly.Plant physiology · 2019Article
- Pathogenic mutations in NUBPL affect complex I activity and cold tolerance in the yeast model Yarrowia lipolytica.Human molecular genetics · 2018Article
- Clinical and genetic aspects of defects in the mitochondrial iron-sulfur cluster synthesis pathway.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Iron-sulfur cluster biosynthesis and trafficking - impact on human disease conditions.Metallomics : integrated biometal science · 2018Review
- Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.The Journal of biological chemistry · 2017Review
- Formation of Nitrogenase NifDK Tetramers in the Mitochondria of Saccharomyces cerevisiae.ACS synthetic biology · 2017Article
- Co-ordination of NDH and Cup proteins in CO2 uptake in cyanobacterium Synechocystis sp. PCC 6803.Journal of experimental botany · 2017Article
Corrections and comments
- Erratum issuedCorrection.2013
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
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 (35)S-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.
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