Protein Folding in Vivo and Renaturation of Recombinant Proteins from Inclusion Bodies

Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology

Volumn 6, Issue 1, 1996, Pages 53-64

  Guise, Andrew D ^b   West, Shauna M ^b   Chaudhuri, Julian B ^a  

^a UNIVERSITY OF BATH   (United Kingdom)

^b NONE

Author keywords

Arginine; Inclusion bodies; Molecular chaperones; Multisubunits; Polyethylene glycol; Protein refolding

Indexed keywords

ESCHERICHIA COLI; EUKARYOTA;

HYBRID PROTEIN;

CELL INCLUSION; CHEMISTRY; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; PROTEIN FOLDING; REVIEW;

HUMANS; INCLUSION BODIES; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS;

EID: 0030204090     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02762323     Document Type: Review

References (67)

1. Marston, F. A. O. (1986) The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 240, 1-12.
2. Kane, J. F. and Hartley, D. L (1988) Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotech. 6, 95-101.
3. Georgiou, G. and Bowden, G. (1991) Inclusion body formation and the recovery of aggregated recombinant proteins, in Recombinant DNA Technology and Applications (Prokop, A., Bajpai, R. K., and Ho, C. S., eds.), McGraw-Hill, USA, pp. 333-356.
4. Freedman, R. B. (1992) Protein folding in the cell, in Protein Folding (Creighton, T. E, ed), W. H. Freeman and Co, New York, pp. 455-540.
5. Schein, C. H. (1989) Production of soluble recombinant proteins in bacteria. Bio/Technol. 7, 1141-1148.
6. Thatcher, D. R. and Hitchcock, A. (1994) Protein folding in biotechnology, in Mechanisms of Protein Folding (Pain, R. H, ed.), IRL, Oxford University Press, Oxford, UK, pp. 229-261.
7. Hlodan, R., Craig, S., and Pain, R. H. (1991) Protein folding and its implications for the production of recombinant proteins. Biotechnol. Genet. Eng. Rev. 9, 47-88.
8. Privalov, P. L (1992) Physical basis of the stability of the folded conformations of proteins, in Protein Folding (Creighton, T. E, ed), W. H. Freeman, NY, pp. 83-126.
9. Gilbert, H. F. (1994) The formation of native disulphide bonds, in Mechanisms of Protein Folding (Pain, R. H., ed.), IRL/Oxford University Press, Oxford, UK, pp. 104-136.
10. Gething M. J., McCammon, K., and Sambrook, J. (1989) Protein folding and intracellular transport evaluation of conformational changes in nascent exocytotic proteins. Meth. Cell. Biol. 32, 185-206.
11. Bochkareva, E. S., Lissin, N. M., and Girshovich, A. S. (1988) Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 336, 254-257.
12. Mitraki, A., Haase-Pettingell, C., and King, J. (1991) Mechanisms of inclusion body formation, in Protein Refolding (De Bernardez-Clark, E. and Georgiou, G, eds.), ACS. Symposium Series, vol. 470: American Chemical Society, Washington, DC, pp. 35-49.
13. Haase-Pettingell, C. and King, J. (1988) Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation: A model for inclusion body formation, J. Biol. Chem. 263, 4977-4983.
14. Sturtevant, J. M., Yu, M.-H., Haase-Pettingell, C., and King, J. (1989) Thermostability of temperature-sensitive folding mutants of the p22 tailspike protein. J. Biol. Chem. 264, 10,693-10,698.
15. Jaenicke, R. (1987) Folding and association of proteins. Prog. Biophys. Mol. Biol. 49, 117-237.
16. Jaenicke, R. and Rudolph, R. (1986) Refolding and association of oligomeric proteins. Methods Enzvmol. 131, 218-250.
17. Seckler, R. and Jaenicke, R. (1992) Protein folding and protein refolding. FASEB J. 6, 2545-2552.
18. Ellis, R. J. (1990) Molecular Chaperones: The plant connection. Science 250, 954-959.
19. Ellis, R. J. (1990) The molecular chaperone concept. Semin. Cell Biol. 1, 72.
20. Hendrick, J. P. and Hartl, F.-U. (1993) Molecular Chaperone functions of heat shock proteins Annu. Rev. Biochem. 62, 349-384.
21. Linquist, S. and Craig, E. (1988) The heat shock proteins. Annu. Rev. Genet. 22, 631-637.
22. Fayet, O., Ziegelhoffer, T., and Georgopoulos, C. (1989) The GroES and GroEL shock gene products of E. coli are essential for bacterial growth at all temperatures. Can. J. Bact. 171, 1379-1385.
23. Beckman, R., Mizzen, L., and Welch, W. (1990) Interaction of Hsp 70 with newly synthesized proteins: implications for proteins folding and assembly. Science 248, 850-854.
24. Chirico, W., Waters, M., and Blobel, G. (1988) 70K Heat shock related proteins stimulate translocation into microsomes. Nature 332, 805-809.
25. Murakami, H., Pain, D., and Blobel, G. (1988) 70 KD heat shock protein is one of at least two factors stimulating protein import into mitochondria. J. Biol. Chem. 107, 2051-2057.
26. Pelham, H. (1986) Speculations on the functions of the major heat-shock and glucose related functions. Cell 46, 959-961.
27. Skowyra, D., Georgopoulos, C., and Zylic, M. (1990) The E. coli DnaK gene product, the hsp 70 homolog, can reactivate the heat inactivated RNA. polymerase in an ATP dependent manner. Cell 62, 939-944.
28. Ellis, R. J. and van der Vies, S. M. (1991) Molecular chaperones. Annu. Rev. Biochem. 60, 321-347.
29. Freedman, R. B. (1991) Protein-disulphide isomerase, in Conformation and Forces in Protein Folding (Nall, B. T. and Dill, K. A., eds.), AAAS, Washington, DC, pp. 204-214.
30. Goldenberg, D. P. (1992) Mutational analysis of protein folding and stability, in Protein Folding (Creighton, T. C, ed), W. H. Freeman and Co, New York, pp. 353-403.
31. Wickner, S., Hoskins, J., and McKenny, K. (1991) Function of DnaJ, and DnaK as chaperones in the origin specific DNA. binding by RePA. Nature 350, 165-167.
32. Ellis, R. and Hemmingsen, S. (1989) Molecular Chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 14, 339-342.
33. Georgopolous, C. and Ang, D. (1990) The E. coli GroE chaperonins. Semin. Cell. Biol. 1, 19-25.
34. Hendrix, R. (1979) Purification and properties of GroE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129, 375-392.
35. McMullin, T. and Hallberg, R. (1988) Molecular. A highly evolutionary conserved mitochondrial protein is structurally related to the protein encoded by E. coli GroEL gene. Cell. Biol. 8, 317-380.
36. Chandrasekhar, G., Tilly, K., Woolford, C., Hendrix, R., and Georgopolous, C. (1986) Purification and properties of the GroES morphenogenic protein of E. coli. J. Biol. Chem. 261, 12,414-12,419.
37. Jaenicke, R. (1993) Role of accessory proteins in protein folding. Curr. Opin. Struct. Biol. 3, 104-112.
38. Miller, A., Maghlaoui, K., Albanese, G., Kleinjan, G., and Smith, C. (1993) E. coli chaperonins Cpn 60 and Cpn 10 do not catalyse the refolding of mitochondrial malate dehydrogenase. Biochem. J. 291, 139-144.
39. Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F. X., and Keifhaber, T, (1991) GroE. facilities refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586-1591.
40. Martin, J. Langer, T., Boteva, R., Schramel, A., and Horwich, A. (1991) Chaperonin mediated protein folding at the surface of GroEL through a molten globule like intermediate. Nature 352, 36-42.
41. Staniforth, R. A., Burston, S. G., Atkinson, T., and Clarke, A. R. (1994) Affinity of chaperonin 60 for a protein substrate and its modulation by nucleotides and chaperonin 10. Biochem. J. 300, 651-658.
42. Mizobata, T., Akiyama, Y., Ito, K., Yumoto, M. and Kawata, Y. (1992) Effects of the chaperonin GroE on the refolding of trytophanase from E. coli. Refolding is enhanced in the prescence of ADP. J. Biol. Chem. 267, 17,773-17,779.
43. Wiech, C. Buchner, J. Zimmermann, R. Jacob, U. (1992) Hsp 90 chaperones: protein folding in vitro. Nature 358, 169,170.
44. London, J., Skrzynia, C., and Goldberg, M. E. (1974) Renaturation of Escherichia coli tryptophanase after exposure to 8M urea. Eur. J. Biochem. 47, 409-415.
45. Goldberg, M. E, Rudloph, R., and Jaenicke, R. (1991) A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochem. 30, 2790-2797.
46. Thatcher, D. R., Wilks, P., and Chaudhuri, J. B. (1996) Inclusion bodies and refolding, in Proteins Labfax (Price, N., ed.), BIOS Scientific, Oxford, pp. 119-130.
47. Babbitt, P. C., West, B. L., Buechter, D. D., Kuntz, I. D., and Kenyon, G. L. (1990) Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Bio/ Technol. 8, 945-949.
48. Rudolph, R. (1990) Renaturation of recombinant, disulphide-bonded proteins from "inclusion bodies," in Modern Methods in Protein- and Nucleic Acid Research (Tschesche, H., ed.), Walter de Gruyter, Berlin, pp. 149-171.
49. Forman, S. M., De Bernardez, E. R., Feldberg, R. S., and Swartz, R. W. (1990) Cross-flow filtration for the separation of inclusion bodies from soluble proteins in Escherichia coli cell lysates. J. Membr. Sci. 48, 263-279.
50. Chaudhuri, J. B. (1994) Refolding recombinant proteins: process strategies and novel approaches. Ann. NY Acad. Sci. 721, 374-385.
51. Vicik, S. and De Bernardez-Clark, E. (1991) An engineering approach to achieving high-protein refolding yields, in ACS Symposium Series, vol. 470: Protein Refolding (De Bernardez-Clark, E. and Georgiou, G., eds.), American Chemical Society, Washington, DC, pp. 180-196.
52. Builder, S. E., and Ogez, J. R. (1984) Purification and activity assurance of precipitated heterologous proteins. US Patent 4620948.
53. Fischer, B., Sumner, I., and Goodenough, P. (1993) Renaturation of lysozyme-temperature dependence of renaturation rate, renaturation yield and aggregation: identification of hydrophobic folding intermediates. Arch. Biochem. Biophys. 306, 183-187.
54. Jaenicke, R. and Rudolph, R. (1989) Folding proteins, in Protein Structure - A Practical Approach (Creighton, T. E. ed.), IRL/Oxford, UK, pp. 191-223.
55. Mendoza, J. A., Rogers, E., Lorimer, G. H., and Horowitz, P. M. (1991) Unassisted refolding of urea unfolded rhodanese. J. Biol. Chem. 266, 13,587-13,591.
56. Gatenby, A. A., Viitanen, P. V., and Lorimer, G. H. (1990) Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria. TIBTECH. 8, 345-358.
57. + dependent. Biochemistry 29, 5665-5671.
58. Buchner, J. and Rudolph, R. (1991) Renaturation, purification and characterization of recombinant fab-fragments produced in Escherichia coli. Bio/Technology 9, 157-162.
59. Seckler, R., Fuchs, A., King, J., and Jaenicke, R. (1989) Reconstitution of the thermostable trimeric phage-P22 tailspike protein from denatured chains in vitro. J. Biol. Chem. 246, 11,750-11,753.
60. Tsou, C.-L. (1986) Location of the active sites of some enzymes in limited and flexible molecular regions. Trends Biochem. Sci. 11, 427-429.
61. Tsou, C.-L. (1993) Conformational flexibility of enzyme active sites. Science 262, 380,381.
62. Cleland, J. L (1993) Impact of protein folding on biotechnology, In ACS Symposium Series, vol. 526: Protein Folding (Cleland, J. L, ed.), American Chemical Society, Washington, DC, pp. 1-21.
63. Rudolph, R, Opitz, U, Hesse, F, Riebland, R., and Fischer, S. (1992) Reactivation of microbially produced human tissue-type plasminogen activator. Biotechnol. Int. 321-325.
64. Cleland, J. L. and Wang, D. I. C. (1990) Cosolvent assisted protein refolding. Bio/Technol. 8, 1274-1278.
65. Cleland, J. L., Builder, S. E., Swartz, J. R., Winkler, M., Chang, J. Y., and Wang, D. J. C. (1992) Polyethylene glycol enhanced protein refolding. Bio/Technol. 10, 1013-1019.
66. Carlson, J. D. and Yarmush, M. L (1992) Antibody assisted protein refolding. Bio/Technol. 10, 86-91.
67. Buchner, J., Brinkmann, U., and Pastan, I. (1992) Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulphide isomerase. Bio/Technol. 10, 682-685.