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Gene Review

NDI1  -  NADH-ubiquinone reductase (H(+)...

Saccharomyces cerevisiae S288c

Synonyms: Internal NADH dehydrogenase, NADH:ubiquinone reductase (non-electrogenic), Rotenone-insensitive NADH-ubiquinone oxidoreductase, mitochondrial, YM7056.06C, YML120C
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Disease relevance of NDI1


High impact information on NDI1


Biological context of NDI1


Anatomical context of NDI1


Associations of NDI1 with chemical compounds

  • Furthermore, striatal concentrations of dopamine and its metabolites in the hemisphere that received rAAV-NDI1 were substantially higher than those of the untreated hemisphere, reaching more than 50% of the normal levels [1].
  • The Ndi1 enzyme is insensitive to complex I inhibitors such as rotenone and 1-methyl-4-phenylpyridinium ion, known as a metabolite of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [1].
  • The cells expressing the Ndi1 protein were resistant to known inhibitors of complex I, such as rotenone and pyridaben [11].
  • Two alternative mechanisms for reoxidizing cytosolic NADH are discussed: (i) cytosolic production of ethanol followed by its intramitochondrial oxidation and (ii) a redox shuttle linking cytosolic NADH oxidation to the internal NADH dehydrogenase [12].
  • The Ndi1 expression scarcely induced an inflammatory response as assessed by hematoxylin and eosin (H&E) staining [13].

Other interactions of NDI1

  • However, when both ADH3 and NDI1 were deleted, metabolism became respirofermentative, indicating that the ethanol-acetaldehyde shuttle is essential for respiratory growth of the ndi1 delta mutant [14].

Analytical, diagnostic and therapeutic context of NDI1


  1. In vivo complementation of complex I by the yeast Ndi1 enzyme. Possible application for treatment of Parkinson disease. Seo, B.B., Nakamaru-Ogiso, E., Flotte, T.R., Matsuno-Yagi, A., Yagi, T. J. Biol. Chem. (2006) [Pubmed]
  2. Molecular remedy of complex I defects: rotenone-insensitive internal NADH-quinone oxidoreductase of Saccharomyces cerevisiae mitochondria restores the NADH oxidase activity of complex I-deficient mammalian cells. Seo, B.B., Kitajima-Ihara, T., Chan, E.K., Scheffler, I.E., Matsuno-Yagi, A., Yagi, T. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  3. Functional expression of the single subunit NADH dehydrogenase in mitochondria in vivo: a potential therapy for complex I deficiencies. Seo, B.B., Nakamaru-Ogiso, E., Cruz, P., Flotte, T.R., Yagi, T., Matsuno-Yagi, A. Hum. Gene Ther. (2004) [Pubmed]
  4. Rotenone-insensitive internal NADH-quinone oxidoreductase of Saccharomyces cerevisiae mitochondria: the enzyme expressed in Escherichia coli acts as a member of the respiratory chain in the host cells. Kitajima-Ihara, T., Yagi, T. FEBS Lett. (1998) [Pubmed]
  5. 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. Mol. Biol. Cell (2006) [Pubmed]
  6. The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. Luttik, M.A., Overkamp, K.M., Kötter, P., de Vries, S., van Dijken, J.P., Pronk, J.T. J. Biol. Chem. (1998) [Pubmed]
  7. Modulation of oxidative phosphorylation of human kidney 293 cells by transfection with the internal rotenone-insensitive NADH-quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae. Seo, B.B., Matsuno-Yagi, A., Yagi, T. Biochim. Biophys. Acta (1999) [Pubmed]
  8. The single subunit NADH dehydrogenase reduces generation of reactive oxygen species from complex I. Seo, B.B., Marella, M., Yagi, T., Matsuno-Yagi, A. FEBS Lett. (2006) [Pubmed]
  9. Mechanism of toxicity in rotenone models of Parkinson's disease. Sherer, T.B., Betarbet, R., Testa, C.M., Seo, B.B., Richardson, J.R., Kim, J.H., Miller, G.W., Yagi, T., Matsuno-Yagi, A., Greenamyre, J.T. J. Neurosci. (2003) [Pubmed]
  10. Lack of complex I activity in human cells carrying a mutation in MtDNA-encoded ND4 subunit is corrected by the Saccharomyces cerevisiae NADH-quinone oxidoreductase (NDI1) gene. Bai, Y., Hájek, P., Chomyn, A., Chan, E., Seo, B.B., Matsuno-Yagi, A., Yagi, T., Attardi, G. J. Biol. Chem. (2001) [Pubmed]
  11. A single-subunit NADH-quinone oxidoreductase renders resistance to mammalian nerve cells against complex I inhibition. Seo, B.B., Nakamaru-Ogiso, E., Flotte, T.R., Yagi, T., Matsuno-Yagi, A. Mol. Ther. (2002) [Pubmed]
  12. In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. Overkamp, K.M., Bakker, B.M., Kötter, P., van Tuijl, A., de Vries, S., van Dijken, J.P., Pronk, J.T. J. Bacteriol. (2000) [Pubmed]
  13. Can a single subunit yeast NADH dehydrogenase (Ndi1) remedy diseases caused by respiratory complex I defects? Yagi, T., Seo, B.B., Nakamaru-Ogiso, E., Marella, M., Barber-Singh, J., Yamashita, T., Kao, M.C., Matsuno-Yagi, A. Rejuvenation research. (2006) [Pubmed]
  14. The mitochondrial alcohol dehydrogenase Adh3p is involved in a redox shuttle in Saccharomyces cerevisiae. Bakker, B.M., Bro, C., Kötter, P., Luttik, M.A., van Dijken, J.P., Pronk, J.T. J. Bacteriol. (2000) [Pubmed]
  15. Possibility of transkingdom gene therapy for complex I diseases. Yagi, T., Seo, B.B., Nakamaru-Ogiso, E., Marella, M., Barber-Singh, J., Yamashita, T., Matsuno-Yagi, A. Biochim. Biophys. Acta (2006) [Pubmed]
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