Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae

W. Curtis Small, Lee McAlister-Henn

Research output: Contribution to journalArticle

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Abstract

The reoxidation of NADH generated in reactions within the mitochondrial matrix of Saccharomyces cerevisiae is catalyzed by an NADH dehydrogenase designated Ndi1p (C. A. M. Marres, S. de Vries, and L. A. Grivell, Eur. J. Biochem. 195:857-862, 1991). Gene disruption analysis was used to examine possible metabolic functions of two proteins encoded by open reading frames having significant primary sequence similarity to Ndi1p. Disruption of the gene designated NDH1 results in a threefold reduction in total mitochondrial NADH dehydrogenase activity in cells cultivated with glucose and in a fourfold reduction in the respiration of isolated mitochondria with NADH as the substrate. Thus, Ndh1p appears to be a mitochondrial dehydrogenase capable of using exogenous NADH. Disruption of a closely related gene designated NDH2 has no effect on these properties. Growth phenotype analyses suggest that the external NADH dehydrogenase activity of Ndh1p is important for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. Codisruption of NDH1 and genes encoding malate dehydrogenases essentially eliminates growth on nonfermentable carbon sources, suggesting that the external mitochondrial NADH dehydrogenase and the malate-aspartate shuttle may both contribute to reoxidation of cytosolic NADH under these growth conditions.

Original languageEnglish (US)
Pages (from-to)4051-4055
Number of pages5
JournalJournal of Bacteriology
Volume180
Issue number16
StatePublished - Aug 1998

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NADH Dehydrogenase
NAD
Saccharomyces cerevisiae
Mitochondria
Growth
Genes
Carbon
Malate Dehydrogenase
Aspartic Acid
Open Reading Frames
Oxidoreductases
Respiration
Ethanol
Phenotype
Glucose
Proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. / Small, W. Curtis; McAlister-Henn, Lee.

In: Journal of Bacteriology, Vol. 180, No. 16, 08.1998, p. 4051-4055.

Research output: Contribution to journalArticle

Small, W. Curtis ; McAlister-Henn, Lee. / Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. In: Journal of Bacteriology. 1998 ; Vol. 180, No. 16. pp. 4051-4055.
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