Affinity purification and characterization of the Escherichia coli molecular chaperones

Protein Expression and Purification

Volumn 24, Issue 2, 2002, Pages 282-291

  Nam, Seung Hee ^a   Walsh, Marie K ^a  

^a UTAH STATE UNIVERSITY   (United States)

Author keywords

Affinity purification; Carbonic anhydrase B; Casein; Chaperones; Protein refolding

Indexed keywords

ESCHERICHIA COLI;

BACTERIAL PROTEIN; CASEIN; CHAPERONE;

AFFINITY CHROMATOGRAPHY; ARTICLE; CHEMISTRY; ESCHERICHIA COLI; ISOLATION AND PURIFICATION; PROTEIN FOLDING; PROTEIN RENATURATION; WESTERN BLOTTING;

BACTERIAL PROTEINS; BLOTTING, WESTERN; CASEINS; CHROMATOGRAPHY, AFFINITY; ESCHERICHIA COLI; MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEIN RENATURATION;

EID: 0036511221     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1571     Document Type: Article

References (37)

1. Altamirano, M. M., Golbik, R., Zahn, R., Buckle, A. M., and Fersht, A. R. (1997) Refolding chromatography with immobilized mini-chaperones. Proc. Natl. Acad. Sci. USA 94, 3576-3578.
2. Bhakuni, V. (1998) Alcohol-induced molten globule intermediates of proteins: Are they real folding intermediates or off pathway products? Arch. Biochem. Biophys. 357, 274-284.
3. Bochkareva, E. S., Lissin, N. M., Flynn, G. C., Rothman, J. E., and Girshovich, A. S. (1992) Positive cooperativity in the functioning of molecular chaperone GroEL. J. Biol. Chem. 10, 6796-6800.
4. Brunschier, R., Danner, M., and Seckler, R. (1993) Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro. J. Biol. Chem. 268, 2767-2772.
5. Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F. X., and Kiefhaber, T. (1991) GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586-1591.
6. Buchner, J., Pastan, I., and Brinkman, U. (1992) A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 205, 263-270.
7. Buchner, J., Brinkman, U., and Pastan, I. (1992) Renaturation of single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase. Biotechnology 10, 682-685.
8. Cleland, J. L. (1993) Impact of protein folding on biotechnology in "Protein Folding in Vitro and in Vivo" (Cleland, J. L., Ed.), pp. 1-21, ACS Symposium Series 526, Am. Chem. Soc., Washington, DC.
9. Dessauer, C. W., and Bartlett, S. G. (1994) Identification of a chaperonin binding site in a chloroplast precursor protein. J. Biol. Chem. 269, 19766-19776.
10. Evers, M. E., Huhse, B., Titorenko, B. I., Kunau, W. H., Hartl, F. U., Harder, W., and Veenhuis, M. (1993) Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase. FEBS Lett. 321, 32-36.
11. Feldman, D. E., and Frydman, J. (2000) Protein folding in vivo: The importance of molecular chaperones. Curr. Opin. Struct. Biol. 10, 26-33.
12. Gottesman, M. E., and Hendrickson, W. A. (2000) Protein folding and refolding by Escherichia coli chaperones and chaperonins. Curr. Opin. Microbiol. 3, 197-202.
13. Graner, M., Raymond, A., Romney, D., He, L., Whitesell, L., and Katsanis, E. (2000) Immunoprotective activities of multiple chaperone proteins isolated from murine B-cell leukemia/lymphoma. Clin. Cancer Res. 6, 909-915.
14. Hejnæs, K. R., Bayne, S., Nørskov, L., Sørensen, H. H., Thomsen, J., Schäffer, L., Wollmer, A., and Skriver, L. (1992) Development of an optimized refolding process for recombinant Ala-Glu-IGF-1. Protein Eng. 5, 797-806.
15. 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, 47-87.
16. Hoskins, J. R., Singh, K. S., Mauriz, M. R., and Wickner, S. (2000) Protein binding and unfolding by the chaperone clpA and degradation by the protease clpAP. Proc. Natl. Acad. Sci. USA 97, 8892-8897.
17. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 227, 680-684.
18. Langer, T., Pfeifer, G., Martin, J., Baumeister, W., and Hartl, F. U. (1992) Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757-4765.
19. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and Hartl, F. U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 352, 36-42.
20. Martin, J., Horwich, A. F., and Hartl, F U. (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258, 995-998.
21. Maurizi, M. R., Clark, W. P., Katayama, Y., Rudikoff, S., Pumphrey, J., Bowers, B., and Gottesman, S. (1990) Sequence and structure of ClpP, the proteolytic of the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 265, 12536-12545.
22. Nandan, D., Daubenberger, C., Mpimbaza, G., and Pearson, T. W. (1994) A rapid, single-step purification method for immunogenic members of the hsp70 family: Validation and application. J. Immunol. Methods 176, 255-263.
23. Pak, M., and Wickner, S. (1997) Mechanism of protein remodeling by clpA chaperone. Proc. Natl. Acad. Sci. USA 94, 4901-4906.
24. Pfanner, N. (1999) Protein folding: Who chaperones nascent chains in bacteria? Curr. Biol. 9, 720-724.
25. Richerme, G., and Kohiyama, M. (1994) Amino acid specificity of the Escherichia coli chaperone GroEL, heat shock protein 60. J. Biol. Chem. 269, 7095-7098.
26. Rozeman, D., and Gellman, S. H. (1996) Artificial chaperone-assisted refolding of carbonic anhydase B. J. Biol. Chem. 271, 3478-3487.
27. Sha, B., and Cyr, D. (1999) Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp 40 Sis1. Acta Crystallogr. D. Biol. Crystallogr. 55, 1234-1236.
28. Sherman, M. Y., and Goldberg, A. L. (1991) Formation in vitro of complexes between an abnormal fusion protein and the heat shock proteins from Escherichia coli and mitochondria. J. Bacteriol. 173, 7249-7256.
29. + exchanger interacts with mammalian heat shock proteins. Biochemistry 34, 10412-10420.
30. Swaisgood, H. E. (1996) Characteristics of milk in "Food Chemistry" (Fennema, O. R., Ed.), 3rd ed., pp. 845-853, Dekker, New York.
31. Szabo, A., Langer, T., Schroder, H., Flanagan, J., and Bukau, B. (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91, 10345-10349.
32. Takeda, S., and McKay, D. B. (1996) Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone. Biochemistry 35, 4636-4644.
33. Thomas, J. G., Ayling, A., and Baneyx, F. (1997) Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. Appl. Biochem. Biotechnol. 66, 197-238.
34. Thomas, J. G., and Baneyx, F. (1997) Divergent effects of chaperone overexpression and ethanol supplementation on inclusion body formation in recombinant Escherichia coli. Protein Express. Purif. 11, 289-296.
35. Thompson, M. W., Singh, S. K., and Mauriz, M. R. (1994) Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. J. Biol. Chem. 269, 18209-18215.
36. Walsh, M. K., and Swaisgood, H. E. (1996) Investigating the use of the chymosin-sensitive sequence of kappa-casein as a cleavable linker site in fusion proteins. J. Biotechnol. 45, 235-241.
37. Wojtkowiak, D., Georgopoulos, C., and Zylicz, M. (1993) Isolation and characterization of clpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J. Biol. Chem. 268, 22609-22617.