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    NDI1 NADH-ubiquinone reductase (H(+)-translocating) NDI1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854919, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    In the current investigation the relationship between ROS production and MMP was studied in respiring yeast cells in stationary phase, using diphenyleneiodonium chloride (DPI), an inhibitor of flavin-containing proteins, as well as the mutants deleted for NDE1, NDE2 and NDI1 genes, encoding flavin-containing external and internal NADH dehydrogenases.

    The role of flavin-containing enzymes in mitochondrial membrane hyperpolarization and ROS production in respiring Saccharomyces cerevisiae cells under heat-shock conditions.
    Fedoseeva IV, Pyatrikas DV, Stepanov AV, Fedyaeva AV, Varakina NN, Rusaleva TM, Borovskii GB, Rikhvanov EG., Free PMC Article

    12/22/2018
    Ubiquinone binding site of yeast NADH dehydrogenase Ndi1 has been described.

    Ubiquinone binding site of yeast NADH dehydrogenase revealed by structures binding novel competitive- and mixed-type inhibitors.
    Yamashita T, Inaoka DK, Shiba T, Oohashi T, Iwata S, Yagi T, Kosaka H, Miyoshi H, Harada S, Kita K, Hirano K., Free PMC Article

    12/22/2018
    Ndi1 associations took place with complexes III and IV suggest the formation of respirasome-like structures.

    New complexes containing the internal alternative NADH dehydrogenase (Ndi1) in mitochondria of Saccharomyces cerevisiae.
    Matus-Ortega MG, Cárdenas-Monroy CA, Flores-Herrera O, Mendoza-Hernández G, Miranda M, González-Pedrajo B, Vázquez-Meza H, Pardo JP.

    04/9/2016
    Ndi1 assimilates electrons to the electron transport chain and initiates the respiration process to make ATP, whereas under stresses, it cleaves the toxicity-sequestering N-terminal cap, is released from the mitochondria, and becomes a cell killer.

    Mitochondrial release of the NADH dehydrogenase Ndi1 induces apoptosis in yeast.
    Cui Y, Zhao S, Wu Z, Dai P, Zhou B., Free PMC Article

    05/11/2013
    The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates

    The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates.
    Iwata M, Lee Y, Yamashita T, Yagi T, Iwata S, Cameron AD, Maher MJ., Free PMC Article

    12/22/2012
    Our data indicate a central role for Complex I dysfunction in pink1-associated defects, and our genetic analyses with heterologous ETC enzymes

    The yeast complex I equivalent NADH dehydrogenase rescues pink1 mutants.
    Vilain S, Esposito G, Haddad D, Schaap O, Dobreva MP, Vos M, Van Meensel S, Morais VA, De Strooper B, Verstreken P., Free PMC Article

    06/30/2012
    Perfusion of TAT-Ndi1 before 30 min no-flow ischemia and up to 2 hr reperfusion suppressed ROS production and preserved ATP stores. Importantly, TAT-Ndi1 infused before ischemia reduced infarct size by 62%.

    Xenotransplantation of mitochondrial electron transfer enzyme, Ndi1, in myocardial reperfusion injury.
    Perry CN, Huang C, Liu W, Magee N, Carreira RS, Gottlieb RA., Free PMC Article

    09/3/2011
    the Ndi1 reaction proceeds through a ternary complex (not a ping-pong) mechanism. The bound UQ keeps oxygen away from the reduced flavin.

    Reaction mechanism of single subunit NADH-ubiquinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae: evidence for a ternary complex mechanism.
    Yang Y, Yamashita T, Nakamaru-Ogiso E, Hashimoto T, Murai M, Igarashi J, Miyoshi H, Mori N, Matsuno-Yagi A, Yagi T, Kosaka H., Free PMC Article

    05/21/2011
    Yeast NDI1 expression in Drosophila mitigated the aging associated decline in respiratory capacity and the accompanying increase in mitochondrial reactive oxygen species production, and resulted in decreased accumulation of markers of oxidative damage.

    Expression of the yeast NADH dehydrogenase Ndi1 in Drosophila confers increased lifespan independently of dietary restriction.
    Sanz A, Soikkeli M, Portero-Otín M, Wilson A, Kemppainen E, McIlroy G, Ellilä S, Kemppainen KK, Tuomela T, Lakanmaa M, Kiviranta E, Stefanatos R, Dufour E, Hutz B, Naudí A, Jové M, Zeb A, Vartiainen S, Matsuno-Yagi A, Yagi T, Rustin P, Pamplona R, Jacobs HT., Free PMC Article

    07/26/2010
    report that expression of Ndi1 in fly mitochondria leads to an increase in NADH-ubiquinone oxidoreductase activity, oxygen consumption, and ATP levels.

    Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreductase (Ndi1) extends Drosophila lifespan.
    Bahadorani S, Cho J, Lo T, Contreras H, Lawal HO, Krantz DE, Bradley TJ, Walker DW., Free PMC Article

    06/14/2010
    identify the ubiquinone binding site in Ndi1

    Characterization of the ubiquinone binding site in the alternative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling.
    Murai M, Yamashita T, Senoh M, Mashimo Y, Kataoka M, Kosaka H, Matsuno-Yagi A, Yagi T, Miyoshi H., Free PMC Article

    05/31/2010
    Disruption of NDI1 decreases ROS production and elongates the chronological life span of yeast, accompanied by the loss of survival fitness.

    Yeast AMID homologue Ndi1p displays respiration-restricted apoptotic activity and is involved in chronological aging.
    Li W, Sun L, Liang Q, Wang J, Mo W, Zhou B., Free PMC Article

    01/21/2010
    Oxidative stress was significantly decreased when the cells were transduced with NDI1. Furthermore, mitochondria from the NDI1-transduced cells showed a suppressed rate of ROS formation by the complex I inhibitors

    The single subunit NADH dehydrogenase reduces generation of reactive oxygen species from complex I.
    Seo BB, Marella M, Yagi T, Matsuno-Yagi A.

    01/21/2010
    data suggest that Ndi1 bears at least two distinct Q sites: one for bound Q and the other for catalytic Q.

    Roles of bound quinone in the single subunit NADH-quinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae.
    Yamashita T, Nakamaru-Ogiso E, Miyoshi H, Matsuno-Yagi A, Yagi T.

    01/21/2010
    NDI1 enzyme can improve the oxidative phosphorylation capacity in cells carrying the G11778A mutation and protect the cells from oxidative stress and cell death.

    Yeast NDI1 improves oxidative phosphorylation capacity and increases protection against oxidative stress and cell death in cells carrying a Leber's hereditary optic neuropathy mutation.
    Park JS, Li YF, Bai Y., Free PMC Article

    01/21/2010
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