This Article
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 Nakai, T.
Right arrow Articles by Ohashi, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakai, T.
Right arrow Articles by Ohashi, A.

 Previous Article  |  Next Article 

Mol. Cell. Biol., Aug 1995, 4441-4452, Vol 15, No. 8
Copyright © 1995, American Society for Microbiology

Multiple genes, including a member of the AAA family, are essential for degradation of unassembled subunit 2 of cytochrome c oxidase in yeast mitochondria

T Nakai, T Yasuhara, Y Fujiki and A Ohashi
Meiji Institute of Health Science, Kanagawa, Japan.

Cytochrome c oxidase consists of three mitochondrion- and several nucleus-encoded subunits. We previously found that in a mutant of Saccharomyces cerevisiae lacking nucleus-encoded subunit 4 of this enzyme (CoxIV), subunits 2 and 3 (CoxII and CoxIII), both encoded by the mitochondrial DNA, were unstable and rapidly degraded in mitochondria, presumably because the subunits cannot assemble normally. To analyze the molecular machinery involved in this proteolytic pathway, we obtained four mutants defective in the degradation of unassembled CoxII (osd mutants) by screening CoxIV-deficient cells for the accumulation of CoxII. All of the mutants were recessive and were classified into three different complementation groups. Tetrad analyses revealed that the phenotype of each mutant was caused by a single nuclear mutation. These results suggest strongly that at least three nuclear genes (the OSD genes) are required for this degradation system. Interestingly, degradation of CoxIII was not affected in the mutants, implying that the two subunits are degraded by distinct pathways. We also cloned the OSD1 gene by complementation of the temperature sensitivity of osd1-1 mutants with a COXIV+ genetic background on a nonfermentable glycerol medium. We found it to encode a member of a family (the AAA family) of putative ATPases, which proved to be identical to recently described YME1 and YTA11. Immunological analyses revealed that Osd1 protein is localized to the mitochondrial inner membrane. Disruption of the predicted ATP-binding cassette by site- directed mutagenesis eliminated biological activities, thereby underscoring the importance of ATP for function.


This article has been cited by other articles:

  • Pastor, M. M., Proft, M., Pascual-Ahuir, A. (2009). Mitochondrial Function Is an Inducible Determinant of Osmotic Stress Adaptation in Yeast. J. Biol. Chem. 284: 30307-30317 [Abstract] [Full Text]  
  • Fiumera, H. L., Dunham, M. J., Saracco, S. A., Butler, C. A., Kelly, J. A., Fox, T. D. (2009). Translocation and Assembly of Mitochondrially Coded Saccharomyces cerevisiae Cytochrome c Oxidase Subunit Cox2 by Oxa1 and Yme1 in the Absence of Cox18. Genetics 182: 519-528 [Abstract] [Full Text]  
  • Dunn, C. D., Tamura, Y., Sesaki, H., Jensen, R. E. (2008). Mgr3p and Mgr1p Are Adaptors for the Mitochondrial i-AAA Protease Complex. Mol. Biol. Cell 19: 5387-5397 [Abstract] [Full Text]  
  • Fiumera, H. L., Broadley, S. A., Fox, T. D. (2007). Translocation of Mitochondrially Synthesized Cox2 Domains from the Matrix to the Intermembrane Space. Mol. Cell. Biol. 27: 4664-4673 [Abstract] [Full Text]  
  • Graef, M., Seewald, G., Langer, T. (2007). Substrate Recognition by AAA+ ATPases: Distinct Substrate Binding Modes in ATP-Dependent Protease Yme1 of the Mitochondrial Intermembrane Space. Mol. Cell. Biol. 27: 2476-2485 [Abstract] [Full Text]  
  • Dunn, C. D., Lee, M. S., Spencer, F. A., Jensen, R. E. (2006). A Genomewide Screen for Petite-negative Yeast Strains Yields a New Subunit of the i-AAA Protease Complex. Mol. Biol. Cell 17: 213-226 [Abstract] [Full Text]  
  • Nittler, M. P., Hocking-Murray, D., Foo, C. K., Sil, A. (2005). Identification of Histoplasma capsulatum Transcripts Induced in Response to Reactive Nitrogen Species. Mol. Biol. Cell 16: 4792-4813 [Abstract] [Full Text]  
  • Lefebvre-Legendre, L., Salin, B., Schaeffer, J., Brethes, D., Dautant, A., Ackerman, S. H., di Rago, J.-P. (2005). Failure to Assemble the {alpha}3 {beta}3 Subcomplex of the ATP Synthase Leads to Accumulation of the {alpha} and {beta} Subunits within Inclusion Bodies and the Loss of Mitochondrial Cristae in Saccharomyces cerevisiae. J. Biol. Chem. 280: 18386-18392 [Abstract] [Full Text]  
  • Augustin, S., Nolden, M., Muller, S., Hardt, O., Arnold, I., Langer, T. (2005). Characterization of Peptides Released from Mitochondria: EVIDENCE FOR CONSTANT PROTEOLYSIS AND PEPTIDE EFFLUX. J. Biol. Chem. 280: 2691-2699 [Abstract] [Full Text]  
  • Hanekamp, T., Thorsness, M. K., Rebbapragada, I., Fisher, E. M., Seebart, C., Darland, M. R., Coxbill, J. A., Updike, D. L., Thorsness, P. E. (2002). Maintenance of Mitochondrial Morphology Is Linked to Maintenance of the Mitochondrial Genome in Saccharomyces cerevisiae. Genetics 162: 1147-1156 [Abstract] [Full Text]  
  • Hori, O., Ichinoda, F., Tamatani, T., Yamaguchi, A., Sato, N., Ozawa, K., Kitao, Y., Miyazaki, M., Harding, H. P., Ron, D., Tohyama, M., M Stern, D., Ogawa, S. (2002). Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease. JCB 157: 1151-1160 [Abstract] [Full Text]  
  • Broadley, S. A., Demlow, C. M., Fox, T. D. (2001). Peripheral Mitochondrial Inner Membrane Protein, Mss2p, Required for Export of the Mitochondrially Coded Cox2p C Tail in Saccharomyces cerevisiae. Mol. Cell. Biol. 21: 7663-7672 [Abstract] [Full Text]  
  • Klanner, C., Prokisch, H., Langer, T. (2001). MAP-1 and IAP-1, Two Novel AAA Proteases with Catalytic Sites on Opposite Membrane Surfaces in Mitochondrial Inner Membrane of Neurospora crassa. Mol. Biol. Cell 12: 2858-2869 [Abstract] [Full Text]  
  • Stribinskis, V., Gao, G.-J., Ellis, S. R., Martin, N. C. (2001). Rpm2, the Protein Subunit of Mitochondrial RNase P in Saccharomyces cerevisiae, Also Has a Role in the Translation of Mitochondrially Encoded Subunits of Cytochrome c Oxidase. Genetics 158: 573-585 [Abstract] [Full Text]  
  • Chacinska, A., Boguta, M., Krzewska, J., Rospert, S. (2000). Prion-Dependent Switching between Respiratory Competence and Deficiency in the Yeast nam9-1 Mutant. Mol. Cell. Biol. 20: 7220-7229 [Abstract] [Full Text]  
  • Seo, S., Okamoto, M., Iwai, T., Iwano, M., Fukui, K., Isogai, A., Nakajima, N., Ohashi, Y. (2000). Reduced Levels of Chloroplast FtsH Protein in Tobacco Mosaic Virus-Infected Tobacco Leaves Accelerate the Hypersensitive Reaction. Plant Cell 12: 917-932 [Abstract] [Full Text]  
  • Lindahl, M., Spetea, C., Hundal, T., Oppenheim, A. B., Adam, Z., Andersson, B. (2000). The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein. Plant Cell 12: 419-432 [Abstract] [Full Text]  
  • Kominsky, D. J., Thorsness, P. E. (2000). Expression of the Saccharomyces cerevisiae Gene YME1 in the Petite-Negative Yeast Schizosaccharomyces pombe Converts It to Petite-Positive. Genetics 154: 147-154 [Abstract] [Full Text]  
  • Steglich, G., Neupert, W., Langer, T. (1999). Prohibitins Regulate Membrane Protein Degradation by the m-AAA Protease in Mitochondria. Mol. Cell. Biol. 19: 3435-3442 [Abstract] [Full Text]  
  • Beilharz, T., Suzuki, C. K., Lithgow, T. (1998). A Toxic Fusion Protein Accumulating between the Mitochondrial Membranes Inhibits Protein Assembly in Vivo. J. Biol. Chem. 273: 35268-35272 [Abstract] [Full Text]  
  • Savel'ev, A. S., Novikova, L. A., Kovaleva, I. E., Luzikov, V. N., Neupert, W., Langer, T. (1998). ATP-dependent Proteolysis in Mitochondria. m-AAA PROTEASE AND PIM1 PROTEASE EXERT OVERLAPPING SUBSTRATE SPECIFICITIES AND COOPERATE WITH THE mtHsp70 SYSTEM. J. Biol. Chem. 273: 20596-20602 [Abstract] [Full Text]  
  • Choquet, Y., Stern, D. B., Wostrikoff, K., Kuras, R., Girard-Bascou, J., Wollman, F.-A. (1998). Translation of cytochrome f is autoregulated through the 5' untranslated region of petA mRNA in Chlamydomonas chloroplasts. Proc. Natl. Acad. Sci. USA 95: 4380-4385 [Abstract] [Full Text]  
  • Jonassen, T., Proft, M., Randez-Gil, F., Schultz, J. R., Marbois, B. N., Entian, K.-D., Clarke, C. F. (1998). Yeast Clk-1 Homologue (Coq7/Cat5) Is a Mitochondrial Protein in Coenzyme Q Synthesis. J. Biol. Chem. 273: 3351-3357 [Abstract] [Full Text]  
  • Campbell, C., Thorsness, P. (1998). Escape of mitochondrial DNA to the nucleus in yme1 yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments. J. Cell Sci. 111: 2455-2464 [Abstract]  
  • Akiyama, Y., Kihara, A., Tokuda, H., Ito, K. (1996). FtsH (HflB) Is an ATP-dependent Protease Selectively Acting on SecY and Some Other Membrane Proteins. J. Biol. Chem. 271: 31196-31201 [Abstract] [Full Text]  
  • Lindahl, M., Tabak, S., Cseke, L., Pichersky, E., Andersson, B., Adam, Z. (1996). Identification, Characterization, and Molecular Cloning of a Homologue of the Bacterial FtsH Protease in Chloroplasts of Higher Plants. J. Biol. Chem. 271: 29329-29334 [Abstract] [Full Text]  
  • Lemaire, C., Hamel, P., Velours, J., Dujardin, G. (2000). Absence of the Mitochondrial AAA Protease Yme1p Restores F0-ATPase Subunit Accumulation in an oxa1 Deletion Mutant of Saccharomyces cerevisiae. J. Biol. Chem. 275: 23471-23475 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»