ArticleNature communications2020
Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 89 citations in OpenAlex.
- Article
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- Structural insights into cauliflower mitoribosome in translation state and in association with a late assembly factor.Nature communications · 2025Article
- Disturbed RNA editing in MORF3-deficient Arabidopsis mitochondria leads to impaired assembly of complex I.Plant physiology · 2025Article
- TheMolecules (Basel, Switzerland) · 2025Review
- Kingdom-specific lipid unsaturation calibrates sequence evolution in membrane arm subunits of eukaryotic respiratory complexes.Nature communications · 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
- The flexible chain: regulation of structure and activity of ETC complexes defines rate of ATP synthesis and sites of superoxide generation.Biophysical reviews · 2025Review
- C1-FDX is required for the assembly of mitochondrial complex I and subcomplexes of complex V in Arabidopsis.PLoS genetics · 2024Article
- Plant supercomplex I + III2 structure and function: implications for the growing field.Biochemical Society transactions · 2024Review
- The ascorbate biosynthesis pathway in plants is known, but there is a way to go with understanding control and functions.Journal of experimental botany · 2024Review
- Deciphering the Genomic Characterization of the GGP Gene Family and Expression Verification ofAntioxidants (Basel, Switzerland) · 2024Article
- Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024Article
- Exploring the potential ofFrontiers in plant science · 2024Article
- FTSH PROTEASE 3 facilitates Complex I degradation through a direct interaction with the Complex I subunit PSST.The Plant cell · 2023Article
- Mitochondrial respiratory complex I proteostasis: The role of a subunit turnover rate.The Plant cell · 2023Article
- The biogenesis and regulation of the plant oxidative phosphorylation system.Plant physiology · 2023Review
- Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae.Nature communications · 2023Article
- Mitochondrial ferredoxin-like is essential for forming complex I-containing supercomplexes in Arabidopsis.Plant physiology · 2023Article
- Structure of mycobacterial respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondria are the powerhouses of eukaryotic cells and the site of essential metabolic reactions. Complex I or NADH:ubiquinone oxidoreductase is the main entry site for electrons into the mitochondrial respiratory chain and constitutes the largest of the respiratory complexes. Its structure and composition vary across eukaryote species. However, high resolution structures are available only for one group of eukaryotes, opisthokonts. In plants, only biochemical studies were carried out, already hinting at the peculiar composition of complex I in the green lineage. Here, we report several cryo-electron microscopy structures of the plant mitochondrial complex I. We describe the structure and composition of the plant respiratory complex I, including the ancestral mitochondrial domain composed of the carbonic anhydrase. We show that the carbonic anhydrase is a heterotrimeric complex with only one conserved active site. This domain is crucial for the overall stability of complex I as well as a peculiar lipid complex composed of cardiolipin and phosphatidylinositols. Moreover, we also describe the structure of one of the plant-specific complex I assembly intermediates, lacking the whole P
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