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• W3092932912 abstract "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 D module, in presence of the maturation factor GLDH. GLDH prevents the binding of the plant specific P1 protein, responsible for the linkage of the P P to the P D module." @default.
• W3092932912 created "2020-10-22" @default.
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• W3092932912 date "2020-10-15" @default.
• W3092932912 modified "2023-10-13" @default.
• W3092932912 title "Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM" @default.
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• W3092932912 doi "https://doi.org/10.1038/s41467-020-18814-w" @default.
• W3092932912 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7567890" @default.
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• W3092932912 hasPublicationYear "2020" @default.
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