Advertisement

Heat Shock pp 165-173 | Cite as

Role of HSP60 in Folding/Assembly of Mitochondrial Proteins

  • A. L. Horwich
  • F. U. Hartl
  • M. Y. Cheng

Abstract

It has long been believed that polypeptides in the intact cell assume their biologically active conformations through steps of spontaneous folding (Anfinsen, 1973). A host of in vitro experiments support such behaviour, demonstrating refolding of proteins diluted from urea or guanidine into their biologically active forms (e. g., Sela et al., 1957; Garel et al., 1876). Yet the time required for such reactions is often hours or days, in contrast with only minutes required to produce biologically active polypeptides in intact cells. Further, the concentrations of polypeptide at which one can observe refolding in vitro are usually less than those present in the intact cell. Additionally, only certain proteins can undergo refolding in vitro: in general, proteins with complex domain structure and multiple subunits fail to fold in vitro.

Keywords

Intact Cell Mitochondrial Protein Mutant Complex Ornithine Transcarbamylase Ribulose Bisphosphate Carboxylase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Anfinsen, CB, (1973) Principles that govern the folding of protein chains. Science, 181: 223–230.PubMedCrossRefGoogle Scholar
  2. Barraclough, R and Ellis, RJ, (1980) Protein synthesis in chloroplasts. IX Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated pea chloroplasts. Biochem. Biophys. Acta, 608: 1931.Google Scholar
  3. Chandrasekhar, GN, Tilly, K, Woolford, C, Hendrix, R and Georgopoulos, C, (1986) The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. J. Biol. Chem., 261: 12414–12419.PubMedGoogle Scholar
  4. Cheng, MY, Hartl, FU, Martin, J, Pollock, RA, Kalousek, F, Neupert, W, Hallberg, EM, Hallberg, RL and Horwich, AL, (1989) Mitochondrial heat- shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature, 337: 620–625.PubMedCrossRefGoogle Scholar
  5. Cheng, MY, Hartl, F-U and Horwich, AL, (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature, 348: 455–458.PubMedCrossRefGoogle Scholar
  6. Ellis, RJ, (1987) Proteins as molecular chaperones. Nature, 328: 378–379.PubMedCrossRefGoogle Scholar
  7. Fayet, O, Ziegelhoffer, T and Georgopoulos, C, (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bact., 171: 1379–1385.PubMedGoogle Scholar
  8. Garei, J-R, Nail, BT and Baldwin, RL, (1976) Guanine-unfolded state of ribonuclease A contains both fast- and slow-refolding species. Proc. Natl. Acad. Sci. USA 73: 1853–1857.CrossRefGoogle Scholar
  9. Georgopoulos, CP, Tilly, K and Casjens, SR, (1983) In “Lambda II”. Hendrix, RW, Roberts, JW, Stahl, FW and Weisberg, RA, eds, Cold Spring Harbor Laboratory Press, pp. 279–304.Google Scholar
  10. Gouloubinoff, P, Gatenby, AA and Lorimer, G, (1989a) GroE heat-shock proteins promote assembly of foreign prokaiyotic ribulose bisphosphate carboxylase oligomers in Escherichia coli Nature, 337: 44–47.Google Scholar
  11. Gouloubinoff, P, Christeller, JT, Gatenby, AA and Lorimer, GH, (1989b) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins ana Mg-ATP. Nature, 342: 884–889.CrossRefGoogle Scholar
  12. Hartl, F-U and Neupert, W, (1990) Protein sorting to mitochondria: evolutionary conservations of folding and assembly. Science, 247: 930–938.PubMedCrossRefGoogle Scholar
  13. Hendrix, RW, (1979) Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. J. Mol. Biol., 129: 359–373.CrossRefGoogle Scholar
  14. Jindal, S, Dudani, AK, Singh, B, Harley, CB and Gupta, RS, (1989) Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonin and to the 65kd mycobacterial antigen. Mol. Cell. Biol., 9: 2279–2283.Google Scholar
  15. Kilmartin, JV, Wright, B and Milstein, CJ, (1982) Rat monoclononal antibodies derived by using a new non secreting rat cell line. J. Cell Biol., 93: 576–582.PubMedCrossRefGoogle Scholar
  16. Lubben, TH, Gatenby, AA Donaldson, GK, Lorimer, GH and Viitanen, PV, (1990) Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. Proc. Natl. Acad. Sci. USA 87: 7683–7687.PubMedCrossRefGoogle Scholar
  17. McMullen, TW and Hallberg, RL, (1987) A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophilca. Mol. Cell. Biol., 7: 4414–4423.Google Scholar
  18. McMullen, TW and Hallberg, RL, (1988) A highly evolutionary conserved mitochondrial protein is structurally relateato the protein encoded by the Escherichia coli groEL gene. Mol. Cell. Biol., 8: 371–380.Google Scholar
  19. Ostermann, J, Horwieh, AL, Neupert, W and Hartl, F-U, (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature, 341: 125–130.PubMedCrossRefGoogle Scholar
  20. Prasad, TK, Hack, E and Hallberg, RL, (1990) Function of the maize mitochondrial chaperonin hsp60: specific association between hsp60 and newly synthesized Fl-ATPase alpha subunits. Mol. Cell. Biol., 10: 3979–3986.PubMedGoogle Scholar
  21. Puchkin, AV, Tsuprun,VL, Solovjeva, NA, Shubin, W, Evstgneeva, ZG and Kretovich, WL, (1982) High molecular weight pea leaf protein similar to the groE protein of E. coli Biochim. Biophys. Acta, 704: 379–384.CrossRefGoogle Scholar
  22. Reading, DS, Hallberg, RL and Myers, AM, (1989) Characterization of the yeast hsp60 gene coding for a mitochondrial assembly factor. Nature, 337: 655–659.PubMedCrossRefGoogle Scholar
  23. Rothman, JE, (1989) Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell, 59: 591–601.PubMedCrossRefGoogle Scholar
  24. Sela, M, White, FH and Anflnsen, CB, (1957) Reductive cleavage of disulfide bridges in ribonuclease. Science, 125: 691–695.PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • A. L. Horwich
    • 1
  • F. U. Hartl
    • 1
    • 2
  • M. Y. Cheng
    • 1
  1. 1.Howard Hughes Medical Institute and Department of Human GeneticsYale School of MedicineNew HavenUSA
  2. 2.Institut fur Physiologische Chemie der Universität MünchenMünchen 2Germany

Personalised recommendations