Abstract
A nuclear encoded mitochondrial heat-shock protein hsp60 is required for the assembly into oligomeric complexes of proteins imported into the mitochondrial matrix. hsp60 is a member of the 'chaperonin' class of protein factors, which include the Escherichia coli groEL protein and the Rubisco subunit-binding protein of chloroplasts.
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References
Pfanner, N., Hartl, F.-U. & Neupert, W. Eur. J. Biochem. 175, 205–212 (1988).
Attardi, G. & Schatz, G. A. Rev. Cell Biol. 4, 289–333 (1988).
Hartl, F.-U., Pfanner, N., Nicholson, D. W. & Neupert, W. Biochim. biophys. Acta 988, 1–45 (1989).
Eilers, M. & Schatz, G. Nature 322, 228–232 (1986).
Chen, W.-J. & Douglas, M. G. Cell 49, 651–658 (1987).
Pfanner, M., Tropschug, M. & Neupert, W. Cell 49, 815–823 (1987).
Deshaies, R. J., Koch, B. D., Werner-Washburne, M., Craig, E. & Schekman, R. Nature 332, 800–805 (1988).
Chirico, W. J., Waters, M. G. & Blobel, G. Nature 332, 805–810 (1988).
Zimmermann, R., Sagstetter, M., Lewis, M. J. & Pelham, H. R. B. EMBO J. 7, 2875–2880 (1988).
Pelham, H. R. B. Cell 46, 959–961 (1986).
Pelham, H. R. B. Nature 332, 776–777 (1988).
Deshaies, R. J., Koch, B. D. & Schekman, R. Trends biochem. Sci. 13, 384–388 (1988).
Schleyer, M. & Neupert, W. Cell 43, 339–350 (1985).
Schwaiger, M., Herzog, V. & Neupert, W. J. Cell Biol. 105, 235–246 (1987).
Böhni, P., Gasser, S., Leaver, C. & Schatz, G. in The Organization and Expression of the Mitochondrial Genome (eds Kroon, A. M. & Saccone, C.) 423–433 (Elsevier, North Holland, 1980).
Hawlitschek, G. et al. Cell 53, 795–806 (1988).
Witte, C., Jensen, R. E., Yaffe, M. P. & Schatz, G. EMBO J. 7, 1439–1447 (1988).
Pollock, R. A. et al. EMBO J. 7, 3493–3500 (1988).
Hartl, F.-U., Schmidt, B., Wachter, E., Weiss, H. & Neupert, W. Cell 47, 939–951 (1986).
Hartl, F.-U., Ostermann, J., Guiard, B. & Neupert, W. Cell 51, 1027–1037 (1987).
Hemmingsen, S. M. et al. Nature 333, 330–334 (1988).
McMullin, T. W. & Hallberg, R. L. Molec. cell Biol. 8, 371–380 (1988).
Ellis, R. J. Nature 328, 378–379 (1987).
Georgopoulos, C. P., Hendrix, R. W., Casjens, S. R. & Kaiser, A. D. J. molec. Biol. 76, 45–60 (1973).
Sternberg, N. J. molec. Biol. 76, 25–44 (1973).
Barraclough, R. & Ellis, R. J. Biochim. biophys. Acta 608, 19–31 (1980).
Ellis, R. J. & van der Vies, S. M. Photosynthesis Res. 16, 101–115 (1988).
Cheng, M. Y., Pollock, R. A., Hendrick, J. P. & Horwich, A. Proc. natn. Acad. Sci. U.S.A. 84, 4063–4067 (1987).
Yaffe, M. P. & Schatz, G. Proc. natn. Acad. Sci. U.S.A. 81, 4819–4823 (1984).
Hoogenraad, N. J., Sutherland, T. M. & Howlett, G. J. analyt. Biochem. 101, 97–102 (1980).
Beechey, R. B., Hubbard, S. A., Linnett, P. E., Mitchell, A. D. & Munn, E. A. Bioch. J. 148, 533–537 (1975).
Reading, D. S., Hallberg, R. L. & Myers, A. M. Nature (this issue).
McMullin, T. W. & Hallberg, R. L. Molec. cell. Biol. 7, 4414–4423 (1987).
Tilly, K., Murialdo, H. & Georgopoulos, C. P. Proc. natn. Acad. Sci. U.S.A. 78, 1629–1633 (1981).
Chandrasekhar, G. N., Tilly, K., Woolford, C., Hendrix, R. & Georgopoulos, C. J. biol. Chem. 261, 12414–12419 (1986).
Bochkareva, E. S., Lissin, N. M. & Girshovich, A. S. Nature 336, 254–257 (1988).
Craig, E. A., Kramer J. & Kosic-Smithers, J. Proc. natn. Acad. Sci. U.S.A. 84, 4156–4160 (1987).
Rothman, J. E. & Kornberg, R. D. Nature 322, 209 (1986).
Munro, S. & Pelham, H. R. B. Cell 46, 291–300 (1986).
Kassenbrock, C. K., Garcia, P. D., Walter, P. & Kelly, R. D. Nature 333, 90–93 (1988).
Laemmli, U. K. Nature 227, 680–685 (1970).
Guiard, B. EMBO J. 4, 3265–3272 (1985).
Pelham, H. R. B. & Jackson, R. J. Eur. J. Biochem. 67, 247–256 (1976).
Davis, R. W., Botstein, D. & Roth, J. R. A Manual for Genetic Engineering, Advanced Bacterial Genetics (Cold Spring Harbor Press, Cold Spring Harbor, 1980).
Maniatis, T., Fritsch, E. F. & Sambrook, J. Molecular Cloning (Cold Spring Harbor Press, Cold Spring Harbor, 1982).
Lehrach, H., Diamond, D., Wozney, J. M. & Boedtker, H. Biochemistry 16, 4743–4751 (1977).
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Cheng, M., Hartl, FU., Martin, J. et al. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337, 620–625 (1989). https://doi.org/10.1038/337620a0
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DOI: https://doi.org/10.1038/337620a0
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