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. 1995 Aug;57(2):235–238.

Mitochondrial protein transport--a system in search of mutations.

W A Fenton
PMCID: PMC1801535  PMID: 7668248

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Selected References

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

  1. Fenton W. A., Hack A. M., Kraus J. P., Rosenberg L. E. Immunochemical studies of fibroblasts from patients with methylmalonyl-CoA mutase apoenzyme deficiency: detection of a mutation interfering with mitochondrial import. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1421–1424. doi: 10.1073/pnas.84.5.1421. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Gavel Y., von Heijne G. Cleavage-site motifs in mitochondrial targeting peptides. Protein Eng. 1990 Oct;4(1):33–37. doi: 10.1093/protein/4.1.33. [DOI] [PubMed] [Google Scholar]
  3. Grompe M., Muzny D. M., Caskey C. T. Scanning detection of mutations in human ornithine transcarbamoylase by chemical mismatch cleavage. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5888–5892. doi: 10.1073/pnas.86.15.5888. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hartl F. U., Pfanner N., Nicholson D. W., Neupert W. Mitochondrial protein import. Biochim Biophys Acta. 1989 Jan 18;988(1):1–45. doi: 10.1016/0304-4157(89)90002-6. [DOI] [PubMed] [Google Scholar]
  5. Hartl F. U., Schmidt B., Wachter E., Weiss H., Neupert W. Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase. Cell. 1986 Dec 26;47(6):939–951. doi: 10.1016/0092-8674(86)90809-3. [DOI] [PubMed] [Google Scholar]
  6. Hendrick J. P., Hodges P. E., Rosenberg L. E. Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc Natl Acad Sci U S A. 1989 Jun;86(11):4056–4060. doi: 10.1073/pnas.86.11.4056. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Horwich A. L., Kalousek F., Fenton W. A., Furtak K., Pollock R. A., Rosenberg L. E. The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge. J Cell Biol. 1987 Aug;105(2):669–677. doi: 10.1083/jcb.105.2.669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Horwich A. L., Kalousek F., Fenton W. A., Pollock R. A., Rosenberg L. E. Targeting of pre-ornithine transcarbamylase to mitochondria: definition of critical regions and residues in the leader peptide. Cell. 1986 Feb 14;44(3):451–459. doi: 10.1016/0092-8674(86)90466-6. [DOI] [PubMed] [Google Scholar]
  9. Horwich A. L., Kalousek F., Rosenberg L. E. Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4930–4933. doi: 10.1073/pnas.82.15.4930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Inana G., Chambers C., Hotta Y., Inouye L., Filpula D., Pulford S., Shiono T. Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy. J Biol Chem. 1989 Oct 15;264(29):17432–17436. [PubMed] [Google Scholar]
  11. Isaya G., Fenton W. A., Hendrick J. P., Furtak K., Kalousek F., Rosenberg L. E. Mitochondrial import and processing of mutant human ornithine transcarbamylase precursors in cultured cells. Mol Cell Biol. 1988 Dec;8(12):5150–5158. doi: 10.1128/mcb.8.12.5150. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Isaya G., Kalousek F., Fenton W. A., Rosenberg L. E. Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide. J Cell Biol. 1991 Apr;113(1):65–76. doi: 10.1083/jcb.113.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Isaya G., Kalousek F., Rosenberg L. E. Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase. J Biol Chem. 1992 Apr 15;267(11):7904–7910. [PubMed] [Google Scholar]
  14. Kalousek F., Isaya G., Rosenberg L. E. Rat liver mitochondrial intermediate peptidase (MIP): purification and initial characterization. EMBO J. 1992 Aug;11(8):2803–2809. doi: 10.1002/j.1460-2075.1992.tb05347.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kang P. J., Ostermann J., Shilling J., Neupert W., Craig E. A., Pfanner N. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature. 1990 Nov 8;348(6297):137–143. doi: 10.1038/348137a0. [DOI] [PubMed] [Google Scholar]
  16. Kiebler M., Becker K., Pfanner N., Neupert W. Mitochondrial protein import: specific recognition and membrane translocation of preproteins. J Membr Biol. 1993 Sep;135(3):191–207. doi: 10.1007/BF00211091. [DOI] [PubMed] [Google Scholar]
  17. Kobayashi T., Ogawa H., Kasahara M., Shiozawa Z., Matsuzawa T. A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor. Am J Hum Genet. 1995 Aug;57(2):284–291. [PMC free article] [PubMed] [Google Scholar]
  18. Kraus J. P., Novotný J., Kalousek F., Swaroop M., Rosenberg L. E. Different structures in the amino-terminal domain of the ornithine transcarbamylase leader peptide are involved in mitochondrial import and carboxyl-terminal cleavage. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8905–8909. doi: 10.1073/pnas.85.23.8905. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ledley F. D., Jansen R., Nham S. U., Fenton W. A., Rosenberg L. E. Mutation eliminating mitochondrial leader sequence of methylmalonyl-CoA mutase causes muto methylmalonic acidemia. Proc Natl Acad Sci U S A. 1990 Apr;87(8):3147–3150. doi: 10.1073/pnas.87.8.3147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Pfanner N., Craig E. A., Meijer M. The protein import machinery of the mitochondrial inner membrane. Trends Biochem Sci. 1994 Sep;19(9):368–372. doi: 10.1016/0968-0004(94)90113-9. [DOI] [PubMed] [Google Scholar]
  21. Pfanner N., Neupert W. The mitochondrial protein import apparatus. Annu Rev Biochem. 1990;59:331–353. doi: 10.1146/annurev.bi.59.070190.001555. [DOI] [PubMed] [Google Scholar]
  22. Schneider H. C., Berthold J., Bauer M. F., Dietmeier K., Guiard B., Brunner M., Neupert W. Mitochondrial Hsp70/MIM44 complex facilitates protein import. Nature. 1994 Oct 27;371(6500):768–774. doi: 10.1038/371768a0. [DOI] [PubMed] [Google Scholar]
  23. Stuart R. A., Cyr D. M., Craig E. A., Neupert W. Mitochondrial molecular chaperones: their role in protein translocation. Trends Biochem Sci. 1994 Feb;19(2):87–92. doi: 10.1016/0968-0004(94)90041-8. [DOI] [PubMed] [Google Scholar]
  24. Sztul E. S., Hendrick J. P., Kraus J. P., Wall D., Kalousek F., Rosenberg L. E. Import of rat ornithine transcarbamylase precursor into mitochondria: two-step processing of the leader peptide. J Cell Biol. 1987 Dec;105(6 Pt 1):2631–2639. doi: 10.1083/jcb.105.6.2631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ungermann C., Neupert W., Cyr D. M. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science. 1994 Nov 18;266(5188):1250–1253. doi: 10.1126/science.7973708. [DOI] [PubMed] [Google Scholar]
  26. Vockley J., Nagao M., Parimoo B., Tanaka K. The variant human isovaleryl-CoA dehydrogenase gene responsible for type II isovaleric acidemia determines an RNA splicing error, leading to the deletion of the entire second coding exon and the production of a truncated precursor protein that interacts poorly with mitochondrial import receptors. J Biol Chem. 1992 Feb 5;267(4):2494–2501. [PubMed] [Google Scholar]
  27. von Heijne G., Steppuhn J., Herrmann R. G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem. 1989 Apr 1;180(3):535–545. doi: 10.1111/j.1432-1033.1989.tb14679.x. [DOI] [PubMed] [Google Scholar]

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