4
Views
11
CrossRef citations to date
0
Altmetric
Research Article

The Yeast F1-ATPase β Subunit Precursor Contains Functionally Redundant Mitochondrial Protein Import Information

, &
Pages 4038-4047 | Received 16 Jun 1987, Accepted 14 Aug 1987, Published online: 31 Mar 2023

LITERATURE CITED

  • Allison, D. S., and G. Schatz. 1986. Artificial mitochondrial presequences. Proc. Natl. Acad. Sci. USA 83:9011–9015.
  • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
  • Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179–207.
  • Chen, W.-J., and M. G. Douglas. 1987. Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondrial matrix. Cell 49:651–658.
  • Daum, G., P. C. Bohni, and G. Schatz. 1982. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028–13033.
  • Douglas, M. G., B. L. Geller, and S. D. Emr. 1984. Intracellular targeting and import of an Fl-ATPase β-subunit-β-galactosidase hybrid protein into yeast mitochondria. Proc. Natl. Acad. Sci. USA 81:3983–3987.
  • Douglas, M. G., M. T. McCammon, and A. Vassarotti. 1986. Targeting proteins into mitochondria. Microbiol. Rev. 50:166–178.
  • Dujon, B. 1981. Mitochondrial genetics and functions, p. 505–635. In J. Strathern, E. Jones, and T. Broach (ed.), Molecular biology of the yeast Saccharomyces: life cycle and inheritance. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Eilers, M., W. Oppliger, and G. Schatz. 1987. Both ATP and an energized inner membrane are required to import a purified precursor protein into mitochondria. EMBO J. 6:1073–1077.
  • Emr, S. D., A. Vassarotti, J. Garrett, B. L. Geller, M. Takeda, and M. G. Douglas. 1986. The amino terminus of the yeast Fl-ATPase β-subunit precursor functions as a mitochondrial import signal. J. Cell Biol. 102:523–533.
  • Gasser, S., G. Daum, and G. Schatz. 1982. Import of proteins into mitochondria. Energy-dependent uptake of precursors by isolated mitochondria. J. Biol. Chem. 257:13034–13041.
  • Gillespie, L. L., C. Argan, A. T. Taneja, R. S. Hodges, K. B. Freeman, and G. C. Shore. 1985. A synthetic signal peptide blocks import of precursor proteins destined for the mitochondrial inner membrane or matrix. J. Biol. Chem. 260:16045–16048.
  • Goldring, E. S., L. I. Grossman, D. Krupnick, D. R. Cryer, and J. Marmur. 1970. The petite mutation in yeast. Loss of mitochondrial deoxyribonucleic acid during induction of petites with ethidium bromide. J. Mol. Biol. 52:323–335.
  • Halvorson, H. O., and L. Ellias. 1958. The purification and properties of an α-glucosidase of Saccharomyces italicus Y1225. Biochim. Biophys. Acta 30:28–40.
  • Hase, T., U. Muller, H. Riezman, and G. Schatz. 1984. A 70-kd protein of the yeast mitochondrial outer membrane is targeted and anchored via its extreme amino terminus. EMBO J. 3: 3157–3164.
  • Hay, R., P. Bohni, and S. Gasser. 1984. How mitochondria import proteins. Biochim. Biophys. Acta 779:65–87.
  • Horwich, A. L., F. Kalousek, W. A. Fenton, R. A. Pollock, and L. E. Rosenberg. 1986. Targeting of pre-ornithine transcarbamylase to mitochondria: definition of critical regions and residues in the leader peptide. Cell 44:451–459.
  • Hurt, E., D. S. Allison, U. Muller, and G. Schatz. 1987. Amino-terminal deletions in the presequence of an imported mitochondrial protein block the targeting function and proteolytic cleavage of the presequence at the carboxy terminus. J. Biol. Chem. 262:1420–1424.
  • Hurt, E., B. Pesold-Hurt, K. Suda, W. Oppliger, and G. Schatz. 1985. The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. EMBO J. 4:2061–2068.
  • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
  • Johnson, L. M., V. A. Bankaitis, and S. D. Emr. 1987. Distinct sequence determinants direct intracellular sorting and modification of a yeast vacuolar protease. Cell 48:875–885.
  • Keng, T., E. Alani, and L. Guarente. 1986. The nine aminoterminal residues of β-aminolevulinate synthase direct β-galactosidase into the mitochondrial matrix. Mol. Cell. Biol. 6:355–364.
  • Laris, P. C. 1977. Evidence for the electrogenic nature of the ATP-ADP exchange system in rat liver mitochondria. Biochim. Biophys. Acta 459:110–118.
  • Maccecchini, M.-L., Y. Rudin, G. Blobel, and G. Schatz. 1979. Import of proteins into mitochondria: precursor forms of the extramitochondrially made F1-ATPase subunits in yeast. Proc. Natl. Acad. Sci. USA 76:343–347.
  • Messing, J., and J. Vieira. 1982. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene 19:269–276.
  • Miller, J. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Newman, A. J., R.-J. Lin, S.-C. Cheng, and J. Abelson. 1985. Molecular consequences of specific intron mutations on yeast mRNA splicing in vivo and in vitro. Cell 42:335–344.
  • Ohta, S., and G. Schatz. 1984. A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria. EMBO J. 3:651–657.
  • Pfaff, E., and M. Klingenberg. 1968. Adenine nucleotide translocation of mitochondria. T. Specificity and control. Eur. J. Biochem. 6:66–79.
  • Pfanner, N., and W. Neupert. 1985. Transport of proteins into mitochondria: a potassium diffusion potential is able to drive the import of ADP/ATP carrier. EMBO J. 4:2819–2825.
  • Pfanner, N., and W. Neupert. 1986. Transport of F1-ATPase subunit β into mitochondria depends on both a membrane potential and nucleoside triphosphates. FEBS Lett. 209:152–156.
  • Pilgrim, D., and E. T. Young. 1987. Primary structure requirements for correct sorting of the yeast mitochondrial protein ADHIII to the yeast mitochondrial matrix space. Mol. Cell. Biol. 7:294–304.
  • Pullman, M. E., H. S. Penefsky, A. Datta, and E. Racker. 1960. Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble, dinitrophenyl-stimulated adenosine triphosphatase. J. Biol. Chem. 235:3322–3329.
  • Reid, G. A. 1985. Transport of proteins into mitochondria. Curr. Top. Membr. Transp. 24:295–336.
  • Reid, G. A., and G. Schatz. 1982. Import of proteins into mitochondria. Extramitochondrial pools and post-translational import of mitochondrial protein precursors in vivo. J. Biol. Chem. 257:13062–13067.
  • Richardson, W. D., B. L. Roberts, and A. E. Smith. 1986. Nuclear location signals in polyoma virus large-T. Cell 44: 77–85.
  • Riezman, H., R. Hay, C. Witte, N. Nelson, and G. Schatz. 1983. Yeast mitochondrial outer membrane specifically binds cytoplasmically-synthesized precursors of mitochondrial proteins. EMBO J. 2:1113–1118.
  • Roise, D., S. J. Horvath, J. M. Tomich, J. H. Richards, and G. Schatz. 1986. A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J. 5:1327–1334.
  • Saltzgaber-Muller, J., S. P. Kunapuli, and M. G. Douglas. 1983. Nuclear genes coding for the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the F1-ATPase β subunit. J. Biol. Chem. 258:11465–11470.
  • Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
  • Scileyer, M., and W. Neupert. 1985. Transport of proteins into mitochondria: translocation intermediates spanning contact sites between outer and inner membranes. Cell 43:339–350.
  • Sherman, F., G. R. Fink, and L. W. Lawrepce. 1979. Methods in yeast genetics: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
  • Szekely, E., and D. L. Montgomery. 1984. Glucose represses transcription of Saccharomyces cerevisiae nuclear genes that encode mitochondrial components. Mol. Cell. Biol. 4:939–946.
  • Takeda, M., A. Vassarotti, and M. G. Douglas. 1985. Nuclear genes coding for the yeast mitochondrial adenosine triphosphatase complex. Primary sequence analysis of ATP2 encoding the F1-ATPase β-subunit precursor. J. Biol. Chem. 260:15458–15465.
  • van Loon, A. P. G. M., A. W. Brandli, and G. Schatz. 1986. The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting. Cell 44:801–812.
  • Vassarotti, A., W.-J. Chen, C. Smagula, and M. G. Douglas. 1987. Sequences distal to the mitochondrial targeting sequences are necessary for the maturation of the Fl-ATPase β-subunit precursor in mitochondria. J. Biol. Chem. 262:411–418.
  • Vassarotti, A., R. Stroud, and M. Douglas. 1987. Independent mutations at the amino terminus of a protein act as surrogate signals for mitochondrial import. EMBO J. 6:705–711.
  • von Heijno, G. 1986. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 5:1335–1342.
  • Wharton, D. C., and A. Tzagoloff. 1967. Cytochrome oxidase from beef heart mitochondria. Methods Enzymol. 10:245–250.
  • Wickerham, L. J. 1946. A critical evaluation of the nitrogen assimilation tests commonly used in the classification of yeasts. J. Bacteriol. 52:293–301.
  • Zimmermann, R., U. Paluch, M. Springl, and W. Neupert. 1979. Cell-free synthesis of the mitochondrial ADP-ATP carrier protein of Neurospora crassa. Eur. J. Biochem. 99:247–252.
  • Zwizinski, C., M. Schleyer, and W. Neupert. 1984. Proteinaceous receptors for the import of mitochondrial precursor proteins. J. Biol. Cherm. 259:7850–7856.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.