ArticleThe Journal of biological chemistry2016
NDUFAF5 Hydroxylates NDUFS7 at an Early Stage in the Assembly of Human Complex I.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 58 citations in OpenAlex.
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- Oxidative protein folding in the intermembrane space of human mitochondria.FEBS open bio · 2024Review
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- A two-step mitochondrial import pathway couples the disulfide relay with matrix complex I biogenesis.The Journal of cell biology · 2023Article
- Expanding the genetic spectrum of mitochondrial diseases in Tunisia: novel variants revealed by whole-exome sequencing.Frontiers in genetics · 2023Article
- SARS-CoV-2 mitochondriopathy in COVID-19 pneumonia exacerbates hypoxemia.Redox biology · 2022Article
- Article
- Tackling Dysfunction of Mitochondrial Bioenergetics in the Brain.International journal of molecular sciences · 2021Review
- Optic atrophy-associated TMEM126A is an assembly factor for the ND4-module of mitochondrial complex I.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions.International journal of molecular sciences · 2021Review
- Complexome Profiling-Exploring Mitochondrial Protein Complexes in Health and Disease.Frontiers in cell and developmental biology · 2021Review
- A Novel Variation in the Mitochondrial Complex I Assembly Factor NDUFAF5 Causes Isolated Bilateral Striatal Necrosis in Childhood.Frontiers in neurology · 2021Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Complex I (NADH ubiquinone oxidoreductase) in mammalian mitochondria is an L-shaped assembly of 45 proteins. One arm lies in the inner membrane, and the other extends about 100 Å into the matrix of the organelle. The extrinsic arm contains binding sites for NADH, the primary electron acceptor FMN, and seven iron-sulfur clusters that form a pathway for electrons linking FMN to the terminal electron acceptor, ubiquinone, which is bound in a tunnel in the region of the junction between the arms. The membrane arm contains four antiporter-like domains, energetically coupled to the quinone site and involved in pumping protons from the matrix into the intermembrane space contributing to the proton motive force. Seven of the subunits, forming the core of the membrane arm, are translated from mitochondrial genes, and the remaining subunits, the products of nuclear genes, are imported from the cytosol. Their assembly is coordinated by at least thirteen extrinsic assembly factor proteins that are not part of the fully assembled complex. They assist in insertion of co-factors and in building up the complex from smaller sub-assemblies. One such factor, NDUFAF5, belongs to the family of seven-β-strand S-adenosylmethionine-dependent methyltransferases. However, similar to another family member, RdmB, it catalyzes the introduction of a hydroxyl group, in the case of NDUFAF5, into Arg-73 in the NDUFS7 subunit of human complex I. This modification occurs early in the pathway of assembly of complex I, before the formation of the juncture between peripheral and membrane arms.
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