Purification of recombinant plant and animal GroES homologs: Chloroplast and mitochondrial chaperonin

Methods in Enzymology

Volumn 290, Issue , 1998, Pages 218-230

  Viitanen, Paul V ^a   Bacot, Karen ^a   Dickson, Ramona ^a   Webb, Tom ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; RECOMBINANT PROTEIN;

ARTICLE; CHLOROPLAST; MITOCHONDRION; MOUSE; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; SEQUENCE HOMOLOGY; SPINACH;

ANIMALIA; SPINACIA OLERACEA;

EID: 0031939210     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(98)90021-0     Document Type: Article

References (46)

1. S. M. Hemmingsen, C. Woolford, S. M. van der Vies, K. Tilly, D. T. Dennis, C. P. Georgopoulos, R. W. Hendrix, and R. J. Ellis, Nature (London) 333, 330 (1988).
2. P. Goloubinoff, J. T. Christeller, A. A. Gatenby, and G. H. Lorimer, Nature (London) 342, 884 (1989).
3. A. A. Gatenby and P. V. Viitanen, Annu. Rev. Plant Physiol. Plant Mol. Biol. 45, 469 (1994).
4. J. P. Hendrick and F.-U. Hartl, Annu. Rev. Biochem. 62, 349 (1993).
5. G. S. Jackson, R. A. Staniforth, D. J. Halsall, T. Atkinson, J. J. Holbrook, A. R. Clarke, and S. G. Burston, Biochemistry 32, 2554 (1993).
6. M. J. Todd, P. V, Viitanen, and G. H. Lorimer, Science 265, 659 (1994).
7. P. V. Viitanen, A. A. Gatenby, and G. H. Lorimer, Protein Sci. 1, 363 (1992).
8. J. Buchner, M. Schmidt, M. Fuchs, R. Jaenicke, R. Rudolph, F. X. Schmid, and T. Kiefhaber, Biochemistry 30, 1586 (1991).
9. A. A. Laminet, T. Ziegelhoffer, C. Georgopoulos, and A. Plückthun, EMBO J. 9, 2315 (1990).
10. M. Schmidt, J. Buchner, M. J. Todd, G. H. Lorimer, and P. V. Viitanen, J. Biol. Chem. 269, 10304 (1994).
11. J. Martin, T. Langer, R. Boteva, A. Schramel, A. L. Horwich, and F.-U. Hartl, Nature (London) 352, 36 (1991).
12. J. S. Weissman, Y. Kashi, W. A. Fenton, and A. L. Horwich, Cell 78, 693 (1994).
13. T. H. Lubben, A. A. Gatenby, G. K. Donaldson, G. H. Lorimer, and P. V. Viitanen, Proc. Natl. Acad. Sci. U.S.A. 87, 7683 (1990).
14. D. J. Hartman, N. J. Hoogenraad, R. Condron, and P. B. Høj, Proc. Natl. Acad. Sci. U.S.A. 89, 3394 (1992).
15. P. V. Viitanen, G. H. Lorimer, R. Seetharam, R. S. Gupta, J. Oppenheim, J. O. Thomas, and N. J. Cowan, J. Biol. Chem. 267, 695 (1992).
16. R. Dickson, B. Larsen, P. V. Viitanen, M. B. Tormey, J. Geske, R. Strange, and L. T. Bemis, J. Biol. Chem. 269, 26858 (1994).
17. G. Legname, T. Fossati, G. Gromo, N. Monzini, F. Marcucci, and D. Modena, FEBS Lett. 361, 211 (1995).
18. M. T. Ryan, D. J. Naylor, N. J. Hoogenraad, and P. B. Høj, J. Biol. Chem. 270, 22037 (1995).
19. P. V. Viitanen, G. Lorimer, W. Bergmeier, C. Weiss, M. Kessel, and P. Goloubinoff, Methods Enzymol. 290, Chap. 18 (1998) (this volume).
20. S. M. Hemmingsen and R. J. Ellis, Plant Physiol. 80, 269 (1986).
21. J. E. Musgrove, R. A. Johnson, and R. J. Ellis, Eur. J. Biochem. 163, 529 (1987).
22. U. Bertsch, J. Soll, R. Seetharam, and P. V. Viitanen, Proc. Natl. Acad. Sci U.S.A. 89, 8696 (1992).
23. N. M. Lissin, FEBS Lett. 361, 55 (1995).
24. F. Baneyx, U. Bertsch, C. E. Kalbach, S. M. van der Vies, J. Soll, and A. A. Gatenby, J. Biol. Chem. 270, 10695 (1995).
25. P. V. Viitanen, M. Schmidt, J. Buchner, T. Suzuki, E. Vierling, R. Dickson, G. H. Lorimer, A. Gatenby, and J. Soll, J. Biol. Chem. 270, 18158 (1995).
26. R. S. Boston, P. V. Viitanen, and E. Vierling, Plant Molecular Biology 32, 191 (1996).
27. A. C. Cavanagh and H. Morton, Eur. J. Biochem. 222, 551 (1994).
28. G. N. Chandrasekhar, K. Tilly, C. Woolford, R. Hendrix, and C. Georgopoulos, J. Biol. Chem. 261, 12414 (1986).
29. P. V. Viitanen, T. H. Lubben, J. Reed, P. Goloubinoff, D. P. O'Keefe, and G. H. Lorimer, Biochemistry 29, 5665 (1990).
30. E. V. Koonin and S. M. van der Vies, Trends Biochem. Sci. 20, 14 (1995).
31. S. J. Landry, J. Zeilstra-Ryalls, O. Fayet, C. Georgopoulos, and L. M. Gierasch, Nature (London) 364, 255 (1993).
32. R. Martel, L. P. Cloney, L. E. Pelcher, and S. M. Hemmingsen, Gene 94, 181 (1990).
33. S. J. Pilkington and J. E. Walker, DNA Sequencing 3, 291 (1993).
34. M. T. Ryan, N. J. Hoogenraad, and P. B. Høj, FEBS Lett. 337, 152 (1994).
35. N. Monzini, G. Legname, F. Marcucci, G. Gromo, and D. Modena, Biochim. Biophys. Acta 1218, 478 (1994).
36. S. Gutteridge, G. S. Reddy, and G. H. Lorimer, Biochem. J. 260, 711 (1989).
37. U. K. Laemmli, Nature (London) 227, 680 (1970).
38. D. J. Hartman, N. J. Hoogenraad, R. Condron, and P. B. Høj, Biochim. Biophys. Acta 1164, 219 (1993).
39. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem. 193, 265 (1951).
40. All pH values reported in text are measured at room temperature.
41. Buffer exchange steps are carried out at 4° using PD-10 gel-filtration columns (Pharmacia, Piscataway, NJ), according to manufacturer instructions.
42. Samples are concentrated at 4° using Centriprep-30 and Centricon-30 concentrators (Amicon, Danvers, MA). It should be emphasized that the spinach ch-cpn10 exhibits a strong propensity to adsorb to various surfaces, including the walls of microcentrifuge tubes. This can result in extremely low yields of purified protein if certain precautions are not taken. The greatest losses occur at low ionic strength and pH values greater than pH 7. However, we have found that the inclusion of glycerol (5%, v/v) and NaCl (0.3 M), during sample concentration and storage, greatly enhances recovery.
43. - ions promote the spontaneous folding of Rubisco, thus obviating the need for GroES.
44. J. F. Hunt, A. J. Weaver, S. J. Landry, L. Gierasch, and J. Deisenhofer, Nature (London) 379, 37 (1996).
45. P. V. Viitanen, unpublished observations (1995).
46. M. Kessel and P. V. Viitanen, unpublished observations (1996).