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Journal of Bacteriology, September 2000, p. 4730-4737, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Mitochondrial Alcohol Dehydrogenase Adh3p Is Involved in a Redox Shuttle in Saccharomyces cerevisiae

Barbara M. Bakker,1,dagger Christoffer Bro,1,2 Peter Kötter,3 Marijke A. H. Luttik,1 Johannes P. van Dijken,1 and Jack T. Pronk1,*

Kluyver Laboratory of Biotechnology, Delft University of Technology, NL-2628 BC Delft, The Netherlands1; Center for Process Biotechnology, Department of Biotechnology, Technical University of Denmark, DK-2800, Lyngby, Denmark2; and Institut für Mikrobiologie, Goethe Universität Frankfurt, Biozentrum N250, 60439 Frankfurt, Germany3

Received 17 March 2000/Accepted 12 June 2000

NDI1 is the unique gene encoding the internal mitochondrial NADH dehydrogenase of Saccharomyces cerevisiae. The enzyme catalyzes the transfer of electrons from intramitochondrial NADH to ubiquinone. Surprisingly, NDI1 is not essential for respiratory growth. Here we demonstrate that this is due to in vivo activity of an ethanol-acetaldehyde redox shuttle, which transfers the redox equivalents from the mitochondria to the cytosol. Cytosolic NADH can be oxidized by the external NADH dehydrogenases. Deletion of ADH3, encoding mitochondrial alcohol dehydrogenase, did not affect respiratory growth in aerobic, glucose-limited chemostat cultures. Also, an ndi1Delta mutant was capable of respiratory growth under these conditions. However, when both ADH3 and NDI1 were deleted, metabolism became respirofermentative, indicating that the ethanol-acetaldehyde shuttle is essential for respiratory growth of the ndi1Delta mutant. In anaerobic batch cultures, the maximum specific growth rate of the adh3Delta mutant (0.22 h-1) was substantially reduced compared to that of the wild-type strain (0.33 h-1). This is consistent with the hypothesis that the ethanol-acetaldehyde shuttle is also involved in maintenance of the mitochondrial redox balance under anaerobic conditions. Finally, it is shown that another mitochondrial alcohol dehydrogenase is active in the adh3Delta ndi1Delta mutant, contributing to residual redox-shuttle activity in this strain.

* Corresponding author. Mailing address: Kluyver Laboratory of Biotechnology, Delft University of Technology, Julianalaan 67, NL-2628 BC Delft, The Netherlands. Phone: 31 15 2783214. Fax: 31 15 2782355. E-mail: J.T.Pronk{at}stm.tudelft.nl.

dagger Present address: Molecular Cell Physiology, Vrije Universiteit, BioCentrum Amsterdam, NL-1081 HV Amsterdam, The Netherlands.

Journal of Bacteriology, September 2000, p. 4730-4737, Vol. 182, No. 17
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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