This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Small, W. C.
Right arrow Articles by McAlister-Henn, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Small, W. C.
Right arrow Articles by McAlister-Henn, L.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 1998, p. 4051-4055, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of a Cytosolically Directed NADH Dehydrogenase in Mitochondria of Saccharomyces cerevisiae

W. Curtis Small and Lee McAlister-Henn*

Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78284-7760

Received 1 May 1998/Accepted 9 June 1998

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.


* Corresponding author. Mailing address: Department of Biochemistry, University of Texas Health Science Center, San Antonio, TX 78284-7760. Phone: (210) 567-3782. Fax: 567-6595. E-mail: henn{at}uthscsa.edu.


Journal of Bacteriology, August 1998, p. 4051-4055, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Bunoust, O., Devin, A., Averet, N., Camougrand, N., Rigoulet, M. (2005). Competition of Electrons to Enter the Respiratory Chain: A NEW REGULATORY MECHANISM OF OXIDATIVE METABOLISM IN SACCHAROMYCES CEREVISIAE. J. Biol. Chem. 280: 3407-3413 [Abstract] [Full Text]  
  • Melo, A. M. P., Bandeiras, T. M., Teixeira, M. (2004). New Insights into Type II NAD(P)H:Quinone Oxidoreductases. Microbiol. Mol. Biol. Rev. 68: 603-616 [Abstract] [Full Text]  
  • Valadi, A., Granath, K., Gustafsson, L., Adler, L. (2004). Distinct Intracellular Localization of Gpd1p and Gpd2p, the Two Yeast Isoforms of NAD+-dependent Glycerol-3-phosphate Dehydrogenase, Explains Their Different Contributions to Redox-driven Glycerol Production. J. Biol. Chem. 279: 39677-39685 [Abstract] [Full Text]  
  • Michalecka, A. M., Svensson, A. S., Johansson, F. I., Agius, S. C., Johanson, U., Brennicke, A., Binder, S., Rasmusson, A. G. (2003). Arabidopsis Genes Encoding Mitochondrial Type II NAD(P)H Dehydrogenases Have Different Evolutionary Origin and Show Distinct Responses to Light. Plant Physiol. 133: 642-652 [Abstract] [Full Text]  
  • Sakaki, K., Tashiro, K., Kuhara, S., Mihara, K. (2003). Response of Genes Associated with Mitochondrial Function to Mild Heat Stress in Yeast Saccharomyces cerevisiae. J Biochem 134: 373-384 [Abstract] [Full Text]  
  • Gibson, N., McAlister-Henn, L. (2003). Physical and Genetic Interactions of Cytosolic Malate Dehydrogenase with Other Gluconeogenic Enzymes. J. Biol. Chem. 278: 25628-25636 [Abstract] [Full Text]  
  • Pahlman, I.-l., Larsson, C., Averet, N., Bunoust, O., Boubekeur, S., Gustafsson, L., Rigoulet, M. (2002). Kinetic Regulation of the Mitochondrial Glycerol-3-phosphate Dehydrogenase by the External NADH Dehydrogenase in Saccharomyces cerevisiae. J. Biol. Chem. 277: 27991-27995 [Abstract] [Full Text]  
  • Overkamp, K. M., Bakker, B. M., Kotter, P., Luttik, M. A. H., van Dijken, J. P., Pronk, J. T. (2002). Metabolic Engineering of Glycerol Production in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 68: 2814-2821 [Abstract] [Full Text]  
  • Davidson, J. F., Schiestl, R. H. (2001). Mitochondrial Respiratory Electron Carriers Are Involved in Oxidative Stress during Heat Stress in Saccharomyces cerevisiae. Mol. Cell. Biol. 21: 8483-8489 [Abstract] [Full Text]  
  • Kerscher, S. J., Eschemann, A., Okun, P. M., Brandt, U. (2001). External alternative NADH:ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica. J. Cell Sci. 114: 3915-3921 [Abstract] [Full Text]  
  • Bakker, B. M., Bro, C., Kötter, P., Luttik, M. A. H., van Dijken, J. P., Pronk, J. T. (2000). The Mitochondrial Alcohol Dehydrogenase Adh3p Is Involved in a Redox Shuttle in Saccharomyces cerevisiae. J. Bacteriol. 182: 4730-4737 [Abstract] [Full Text]  
  • Overkamp, K. M., Bakker, B. M., Kötter, P., van Tuijl, A., de Vries, S., van Dijken, J. P., Pronk, J. T. (2000). In Vivo Analysis of the Mechanisms for Oxidation of Cytosolic NADH by Saccharomyces cerevisiae Mitochondria. J. Bacteriol. 182: 2823-2830 [Abstract] [Full Text]  
  • Boubekeur, S., Bunoust, O., Camougrand, N., Castroviejo, M., Rigoulet, M., Guerin, B. (1999). A Mitochondrial Pyruvate Dehydrogenase Bypass in the Yeast Saccharomyces cerevisiae. J. Biol. Chem. 274: 21044-21048 [Abstract] [Full Text]  
  • Kerscher, S., Okun, J., Brandt, U (1999). A single external enzyme confers alternative NADH:ubiquinone oxidoreductase activity in Yarrowia lipolytica. J. Cell Sci. 112: 2347-2354 [Abstract]  
  • Melo, A. M. P., Duarte, M., Moller, I. M., Prokisch, H., Dolan, P. L., Pinto, L., Nelson, M. A., Videira, A. (2001). The External Calcium-dependent NADPH Dehydrogenase from Neurospora crassa Mitochondria. J. Biol. Chem. 276: 3947-3951 [Abstract] [Full Text]