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. 1988 Dec 1;7(12):3857–3862. doi: 10.1002/j.1460-2075.1988.tb03271.x

Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes.

M Yang 1, R E Jensen 1, M P Yaffe 1, W Oppliger 1, G Schatz 1
PMCID: PMC454964  PMID: 2905264

Abstract

We have purified the metalloprotease which is localized in the soluble matrix space of Saccharomyces cerevisiae mitochondria and cleaves the amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins. The enzyme consists of two loosely associated non-identical subunits of mol. wt 48,000 and 51,000, respectively. Attempts to separate the two subunits from each other caused loss of activity. The smaller subunit had been identified as the product of the nuclear MAS1 gene (Witte et al., 1988). The larger subunit is now identified as the product of the nuclear MAS2 gene.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baker R. K., Lively M. O. Purification and characterization of hen oviduct microsomal signal peptidase. Biochemistry. 1987 Dec 29;26(26):8561–8567. doi: 10.1021/bi00400a010. [DOI] [PubMed] [Google Scholar]
  2. Böhni P. C., Daum G., Schatz G. Import of proteins into mitochondria. Partial purification of a matrix-located protease involved in cleavage of mitochondrial precursor polypeptides. J Biol Chem. 1983 Apr 25;258(8):4937–4943. [PubMed] [Google Scholar]
  3. Conboy J. G., Fenton W. A., Rosenberg L. E. Processing of pre-ornithine transcarbamylase requires a zinc-dependent protease localized to the mitochondrial matrix. Biochem Biophys Res Commun. 1982 Mar 15;105(1):1–7. doi: 10.1016/s0006-291x(82)80002-8. [DOI] [PubMed] [Google Scholar]
  4. Daum G., Böhni P. C., Schatz G. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J Biol Chem. 1982 Nov 10;257(21):13028–13033. [PubMed] [Google Scholar]
  5. Eilers M., Schatz G. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature. 1986 Jul 17;322(6076):228–232. doi: 10.1038/322228a0. [DOI] [PubMed] [Google Scholar]
  6. Evans E. A., Gilmore R., Blobel G. Purification of microsomal signal peptidase as a complex. Proc Natl Acad Sci U S A. 1986 Feb;83(3):581–585. doi: 10.1073/pnas.83.3.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gasser S. M., Ohashi A., Daum G., Böhni P. C., Gibson J., Reid G. A., Yonetani T., Schatz G. Imported mitochondrial proteins cytochrome b2 and cytochrome c1 are processed in two steps. Proc Natl Acad Sci U S A. 1982 Jan;79(2):267–271. doi: 10.1073/pnas.79.2.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Haid A., Suissa M. Immunochemical identification of membrane proteins after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Methods Enzymol. 1983;96:192–205. doi: 10.1016/s0076-6879(83)96017-2. [DOI] [PubMed] [Google Scholar]
  9. Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F. U., Neupert W. Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein. Cell. 1988 Jun 3;53(5):795–806. doi: 10.1016/0092-8674(88)90096-7. [DOI] [PubMed] [Google Scholar]
  10. Hurt E. C., Pesold-Hurt B., Schatz G. The amino-terminal region of an imported mitochondrial precursor polypeptide can direct cytoplasmic dihydrofolate reductase into the mitochondrial matrix. EMBO J. 1984 Dec 20;3(13):3149–3156. doi: 10.1002/j.1460-2075.1984.tb02272.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kumamoto T., Ito A., Omura T. Characterization of a mitochondrial matrix protease catalyzing the processing of adrenodoxin precursor. J Biochem. 1986 Jul;100(1):247–254. doi: 10.1093/oxfordjournals.jbchem.a121700. [DOI] [PubMed] [Google Scholar]
  12. McAda P. C., Douglas M. G. A neutral metallo endoprotease involved in the processing of an F1-ATPase subunit precursor in mitochondria. J Biol Chem. 1982 Mar 25;257(6):3177–3182. [PubMed] [Google Scholar]
  13. Miura S., Mori M., Amaya Y., Tatibana M. A mitochondrial protease that cleaves the precursor of ornithine carbamoyltransferase. Purification and properties. Eur J Biochem. 1982 Mar 1;122(3):641–647. [PubMed] [Google Scholar]
  14. Ohashi A., Gibson J., Gregor I., Schatz G. Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent. J Biol Chem. 1982 Nov 10;257(21):13042–13047. [PubMed] [Google Scholar]
  15. Robinson C., Ellis R. J. Transport of proteins into chloroplasts. Partial purification of a chloroplast protease involved in the processing of important precursor polypeptides. Eur J Biochem. 1984 Jul 16;142(2):337–342. doi: 10.1111/j.1432-1033.1984.tb08291.x. [DOI] [PubMed] [Google Scholar]
  16. Schmidt B., Wachter E., Sebald W., Neupert W. Processing peptidase of Neurospora mitochondria. Two-step cleavage of imported ATPase subunit 9. Eur J Biochem. 1984 Nov 2;144(3):581–588. doi: 10.1111/j.1432-1033.1984.tb08505.x. [DOI] [PubMed] [Google Scholar]
  17. Teintze M., Slaughter M., Weiss H., Neupert W. Biogenesis of mitochondrial ubiquinol:cytochrome c reductase (cytochrome bc1 complex). Precursor proteins and their transfer into mitochondria. J Biol Chem. 1982 Sep 10;257(17):10364–10371. [PubMed] [Google Scholar]
  18. Verner K., Schatz G. Protein translocation across membranes. Science. 1988 Sep 9;241(4871):1307–1313. doi: 10.1126/science.2842866. [DOI] [PubMed] [Google Scholar]
  19. Witte C., Jensen R. E., Yaffe M. P., Schatz G. MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease. EMBO J. 1988 May;7(5):1439–1447. doi: 10.1002/j.1460-2075.1988.tb02961.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wolf D. H. Control of metabolism in yeast and other lower eukaryotes through action of proteinases. Adv Microb Physiol. 1980;21:267–338. doi: 10.1016/s0065-2911(08)60358-6. [DOI] [PubMed] [Google Scholar]
  21. Wolfe P. B., Silver P., Wickner W. The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme. J Biol Chem. 1982 Jul 10;257(13):7898–7902. [PubMed] [Google Scholar]
  22. Yaffe M. P., Ohta S., Schatz G. A yeast mutant temperature-sensitive for mitochondrial assembly is deficient in a mitochondrial protease activity that cleaves imported precursor polypeptides. EMBO J. 1985 Aug;4(8):2069–2074. doi: 10.1002/j.1460-2075.1985.tb03893.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yaffe M. P., Schatz G. Two nuclear mutations that block mitochondrial protein import in yeast. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4819–4823. doi: 10.1073/pnas.81.15.4819. [DOI] [PMC free article] [PubMed] [Google Scholar]

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