Chaperone-like activity of tubulin: Binding and reactivation of unfolded substrate enzymes

Journal of Biological Chemistry

Volumn 276, Issue 43, 2001, Pages 39742-39747

  Manna, Tapas ^a   Sarkar, Taradas ^a   Poddar, Asim ^a   Roychowdhury, Manami ^a   Das, Kali P ^a   Bhattacharyya, Bhabatarak ^a  

^a BOSE INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; CHEMICAL BONDS; ENZYMES; PROTEINS; SUBSTRATES; THERMAL STRESS; UREA;

CHAPERONE-LIKE ACTIVITY;

BIOCHEMISTRY;

ALCOHOL DEHYDROGENASE; ALPHA GLUCOSIDASE; CHAPERONE; CYTOSKELETON PROTEIN; GUANIDINE; LACTATE DEHYDROGENASE; TUBULIN; UREA; MALATE DEHYDROGENASE;

ARTICLE; CELL MOTILITY; DIMERIZATION; EUKARYOTE; MICROTUBULE; MITOSIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; STRESS; ENZYME ACTIVATION; HEAT; METABOLISM;

EUKARYOTA;

ALCOHOL DEHYDROGENASE; ALPHA-GLUCOSIDASES; ENZYME ACTIVATION; HEAT; L-LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MOLECULAR CHAPERONES; PROTEIN DENATURATION; PROTEIN FOLDING; TUBULIN;

EID: 0035955639     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M104061200     Document Type: Article

References (39)

1. Gething, M. J. (eds) (1997) Guidebook to Molecular Chaperones and Protein Folding Factors, Oxford University Press, Oxford
2. Hartl, F. U. (1996) Nature 381, 571-580
3. Frydman, J., and Hohfeld, J. (1997) Trends Biochem. Sci. 22, 87-92
4. Netzer, W. J., and Hartl, F. U. (1998) Trends Biochem. Sci. 23, 68-73
5. Ellis, R. J. (1996) Science 272, 1448-1449
6. Guha, S., Manna, T. K., Das, K. P., and Bhattacharyya, B. (1998) J. Biol. Chem. 273, 30077-30080
7. Fenton, W. A., and Horwich, A. L. (1997) Protein Sci. 6, 743-760
8. Martin, J., and Hartl, F. U. (1997) Curr. Opin. Struct. Biol. 7, 41-52
9. Ruddon, R. W., and Bedows, E. (1997) J. Biol. Chem. 272, 3125-3128
10. Sigler, P. B., Xu, Z., Rye, H. S., Burston, S. G., Fenton, W. A., and Horwich, A. L. (1998) Annu. Rev. Biochem. 67, 581-608
11. Hamel, E., and Lin, C. (1981) Arch. Biochem. Biophys. 209, 29-40
12. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
13. Gnagliardi, A., Cerchia, L., and Rossi, M. (1995) J. Biol. Chem. 270, 28126-28132
14. Ranson, N. A., Dunster, N. J., Burston, S. G., and Clarke, A. R. (1995) J. Mol. Biol. 250, 581-586
15. Chattopadhyay, S., Das, B., Bera, A. K., Dasgupta, D., and Dasgupta, C. (1994) Biochem. J. 300, 717-721
16. Kopetzky, E., Schumacher, G., and Buckel, P. (1989) Mol. Gen. Genet. 216, 149-155
17. Bhattacharyya. B., Sackett, D. L., and Wolff, J. (1985) J. Biol. Chem. 260, 10208-10216
18. Muchowski, P. J., Bassuk, J. A., Lubsen, N. H., and Clark, J. H. (1997) J. Biol. Chem. 272, 2578-2582
19. Weich, H., Buchner, J., Zimmermann, R., and Jacob, U. (1992) Nature 358, 169-170
20. Bohen, S. P., and Yamamoto, K. R. (1994) in The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R. I., Tissieres, A., and Georgopulos, C., eds) pp. 313-334, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
21. Jacob, U., Gaestel, M., Engel, K., and Buchner, J. (1993) J. Biol. Chem. 268, 1517-1520
22. Jacob, U., Lilie, H., Meyer, I., and Buchner, J. (1995) J. Biol. Chem. 270, 7288-7294
23. Taguchi, H., Makino, Y., and Yoshida, M. (1994) J. Biol. Chem. 269, 8529-8534
24. Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmidt, F. X., and Kiefhaber, T. (1991) Biochemistry 30, 1586-1591
25. Viitanen, P. V., Lubben, T. H., Reed, J., Goloubinoff, P., O'Keefe, D., and Lorimer, G. H. (1990) Biochemistry 29, 5665-5671
26. Jaenicke, R., and Rudolph, R. (1990) in Protein Structure: A Practical Approach (Creighton, T. E., ed) pp 191-223, IRL Press, Oxford
27. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwicz, A. L., and Hartl, F. U. (1991) Nature 352, 36-42
28. Ward, L. D., and Timasheff, S. N. (1994) Biochemistry 33, 11891-11899
29. Pontingel, H., Krauhs, E., and Little, M. (1983) J. Submicrosc. Cytol. Pathol. 15, 359-362
30. Bhattacharyya, J., and Das, K. P. (1999) J. Biol. Chem. 274, 15505-15509
31. Pal, S., Chandra, S., Chowdhury, S., Sarkar, D., Ghosh, A. N., and Das Gupta, C. (1999) J. Biol. Chem. 274, 32771-32777
32. Jacob, U., and Buchner, J. (1994) Trends Biochem. Sci. 19, 205-211
33. Buchner, J. (1996) FASEB J. 10, 10-19
34. Szebeni, A., and Olson, M. O. J. (1999) Protein Sci. 8, 905-912
35. Yoshida, M., Ishii, N., Muneyuki, E., and Taguchi, H. (1993) Philos. Trans. R. Soc. Lond. B. Biol. Sci. 339, 305-312
36. Zheng, X., Rosenberg, L. E., Kalousek, F., and Fenton, W. A. (1993) J. Biol. Chem 268, 7489-7493
37. Gao, Y., Thomas, J. O., Chow, R. L., Lee, G. H., and Cowan, N. J. (1992) Cell 69, 1043-1050
38. Melki, R., and Cowan, N. J. (1994) Mol. Cell. Biol. 14, 2895-2904
39. Sternlicht, H., Farr, G. W., Sternlicht, M. L., Driscoll, J. K., and Yaffe, M. B. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 9422-9426