Stabilization of human triosephosphate isomerase by improvement of the stability of individual α-helices in dimeric as well as monomeric forms of the protein

Biochemistry

Volumn 35, Issue 13, 1996, Pages 4110-4117

  Mainfroid, Véronique ^a   Mande, Shekhar C ^b   Hol, Wim G J ^b   Martial, Joseph A ^a   Goraj, Karine ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MUTANT PROTEIN; TRIOSEPHOSPHATE ISOMERASE;

AMINO ACID SUBSTITUTION; ARTICLE; ENTROPY; ENZYME STABILITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; CALORIMETRY; ENZYME STABILITY; HUMANS; KINETICS; MACROMOLECULAR SUBSTANCES; MATHEMATICS; MODELS, MOLECULAR; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRIOSE-PHOSPHATE ISOMERASE; UREA;

EID: 0029934644     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952692n     Document Type: Article

References (69)

1. Banner, D. W., Bloomer, A. C., Petsko, G. A., Phillips, D. C., Posson, C. I., Wilson, I. A., Corran, P. H., Furth, A. J., Milman, J. D., Offord, R. E., Priddle, J. D., & Waley, S. G. (1975) Nature 255, 609-614.
2. Blaber, M., Zhang, X. J., & Matthews, B. W. (1993) Science 260, 1637-1640.
3. Blaber, M., Zhang, X. J., Lindstrom, J. L., Pepiot, S. D., Baase, W. A., & Matthews, B. W. (1994) J Mol. Biol. 235, 600-624.
4. Bränden, C. I. (1991) Curr. Opin. Struct. Biol. 1, 978-983.
5. Chakrabarti, P. (1994) Protein Eng. 7, 471-474.
6. Cho, Y., Gu, W., Watkins, S., Lee, S. P., Kim, T. R., Brady, J. W., & Batt, C. A. (1994) Protein Eng. 7, 263-270.
7. Daar, I. A., Artymiuk, P. J., Phillips, D. C., & Maquat, L. E. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7903-7907.
8. Daopin, S., Baase, W. A., & Matthews, B. W. (1990) Proteins: Struct., Funct., Genet. 7, 198-204.
9. Delboni, L. F., Mande, S. C., Rentier-Delrue, F., Mainfroid, V., Turley, S., Vellieux, F. M. D., Martial, J. A., & Hol, W. G. J. (1995) Protein Sci. 4, 2594-2604.
10. Eder, J., & Wilmanns, M. (1992) Biochemistry 31, 4437-4444.
11. Eftink, M. R., Helton, K. J., Beavers, A., & Ramsay, G. D. (1994) Biochemistry 33, 10220-10228.
12. Eriksson, A. E., Baase, W. A., Zhang, X. J., Heinz, D. W., Blaber, M., Baldwin, E. P., & Matthews, B. W. (1992) Science 255, 178-183.
13. Farber, G. K., & Petsko, G. A. (1990) Trends Biochem. Sci. 15, 228-234.
14. Fernando, T., & Royer, C. A. (1992) Biochemistry 31, 6683-6691.
15. Fersht, A. R., & Serrano, L. (1993) Curr. Opin. Struct. Biol. 3, 75-83.
16. Fersht, A. R., Shi, J. P., Knill-Jones, J., Lowe, D. M., Wilkinson, A. J., Blow, D. M., & Brick, P. Nature 314, 235-238.
17. Fontana, A. (1988) Biophys. Chem. 29, 181-193.
18. Fontana, A. (1991) Curr. Opin. Biotechnol. 2, 551-560.
19. Forood, B. Feliciano, E. J., & Nambrai, K. P. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 838-842.
20. Hendsch, Z. C., & Tidor, B. (1994) Protein Sci. 3, 211-226.
21. Herning, T., Yutani, K., Inaka, K., Kuroki, R., Matsushima, M., & Kikuchi, M. (1992) Biochemistry 31, 7077-7085.
22. Ishikawa, K., Kimura, S., Kanaya, S., Morikawa, K., & Nakamura, H. (1993) Protein Eng. 6, 85-91.
23. Jaenicke, R. (1987) Prog. Biophys. Mol. Biol. 49, 117-237.
24. Jaenicke, R. (1991) Biochemistry 30, 3147-3161.
25. Janin, J. (1991) Curr. Opin. Struct. Biol. 1, 42-44.
26. Jones, D. H., Mc Millan, A. J., & Fersht, A. R. (1985) Biochemistry 24, 5852-5857.
27. Jones, S., & Thornton, J. M. (1995) Prog. Biophys. Mol. Biol. 63, 31-65.
28. Kellis, J. T. J., Nyberg, K., & Fersht, A. R. (1988) Biochemistry 28, 4914-4922.
29. Kelly, R. M., & Brown, S. H. (1993) Curr. Opin. Biotechnol. 4, 188-192.
30. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
31. Kuroki, R., Taniyama, Y., Seko, C. Nakamura, H., Kikuchi, M., & Ikehara, M. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6903-6907.
32. Leatherbarrow, R. J. (1987) Enzfitter: A Non-Linear Regression Data Analysis Program for the IBM PC/P52, Elsevier Biosoft, Cambridge, U.K.
33. Lee, E. H., Soper, T. S., Mural, R. J., Stringer, C. D., & Hartman, F. C. (1987) Biochemistry 26, 4599-4604.
34. Lolis, E., Alber, T., Davenport, R. C. Rose, D., Hartmaru F. C., & Petsko, G. A. (1990) Biochemistry 29, 6609-6618.
35. Mainfroid, V., Goraj, K., Rentier-Delrue, F., Houbrechts, A., Loiseau, A., Gohimont, A. C., Noble, M. E. M., Borchert, T. V., Wierenga, R. K., & Martial, J. A. (1993) Protein Eng. 6, 893-900.
36. Mainfroid, V., Terpstra, P., Beauresard, N., Frère, J.-M., Mande, S. C., Hol, W. G. J., Martial, J. A., & Goraj, K. (1996) J. Mol. Biol. 257, 441-456.
37. Mande, S. C., Mainfroid, V., Kalk, K. H., Goraj, K., Martial, J. A., & Hol, W. G. J. (1994) Protein Sci. 3, 810-821.
38. Marqusee, S., & Sauer, R. T. (1994) Protein Sci. 3, 2217-2225.
39. Matsumura, M., Becktel, W. J., & Matthews, B. W. (1988) Nature 344, 406-410.
40. Matthews, B. W. (1991) Curr. Opin. Struct. Biol. 1, 17-21.
41. Matthews, B W., Nicholson, H., & Becktel, W. J. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 6663-6667.
42. Menéndez-Arias, L., & Argos, P. (1989) J. Mol. Biol. 206, 397-406.
43. Mossing, M. C., & Sauer, R. T. (1990) Science 250, 1712-1715.
44. Nicholson, H., Becktel, W. J., & Matthews, B. W. (1988) Nature 336, 651-656.
45. Nicholson, H., Anderson, D. E., Daopin, S., & Matthews, B. W. (1991) Biochemistry 30, 9816-9828.
46. Nicholson, H., Tronrud, D. E., Becktel, W. J., & Matthews, B. W. (1992) Biopolymers 32, 1431-1441.
47. Noble, M. E. M., Zeelen, J. P., Wierenga, R. K., Mainfroid, V., Goraj, K., Gohimont, A. C., & Martial, J. A. (1993) Acta Crystallogr. D49, 403-417.
48. Nordhoff, A., Bücheler, U. S., Werner, D., & Schirmer, R. H. (1993) Biochemistry 32, 4060-4066.
49. Pace, C. N. (1990) Trends Biochem. Sci. 15, 14-17.
50. Pantoliano, M. W., Whitlow, M., Wood, J. F., Rollence, M. L. Finzel, B. C., Gilligard, G. L., Poulos, T. L., & Bryan, P. N. (1988) Biochemistry 27, 8311-8317.
51. Rentier-Delrue, F., Mande, S. C., Moyens, S., Mainfroid, V., Goraj, K., Lion, M., Hol, W. G. J., & Martial, J. A. (1993) J. Mol. Biol. 229, 85-93.
52. Richardson, J. S., & Richardson, D. C. (1988) Science 240, 1648-1652.
53. Rieder, S. V., & Rose, I. A. (1959) J. Biol. Chem. 234, 1007-1010.
54. Sandberg, W. S., & Terwilliger, T. C. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 1706-1710.
55. Schimmel, P. R., & Flory, P. J. (1968) J. Mol. Biol. 34, 105-120.
56. Serrano, L., & Fersht, A. R. (1989) Nature 342, 296-299.
57. Serrano, L., Kellis, J. T., Cann, P., Matouschek, A., & Fersht, A. R. (1992a) J. Mol. Biol. 224, 783-804.
58. Serrano, L., Sancho, J., Hirshberg, M., & Fersht, A. R. (1992b) J. Mol. Biol. 227, 544-559.
59. Serrano, L., Niera, J. L., Sancho, J., & Fersht, A. R. (1992c) Nature 356, 453-455.
60. Shirley, B. A., Stanssens, P., Hahn, U., & Pace, C. N. (1992) Biochemistry 31, 725-732.
61. Studier, F. W., & Moffatt, B. A. (1986) J. Mol. Biol. 189, 113-130.
62. Timm, D. E., & Neet, K. E. (1992) Protein Sci. 1, 236-244.
63. Ueda, T., Tamura, T., Maeda, Y. Hashimoto, Y., Miki, T., Yamada, H., & Imoto, T. (1993) Protein Eng. 6, 183-187.
64. Vriend, G. (1990) J. Mol. Graphics 8, 52-56.
65. Waldburger, C. D., Schildbach, J. F., & Sauer, R. T. (1995) Nature Struct. Biol. 2, 122-128.
66. Wells, J. A. (1990) Biochemistry 29, 8509-8517.
67. Wierenga, R. K., Noble, M. E. M., Vriend, G., Nauche, S., & Hol, W. G. J. (1991) J. Mol. Biol. 220, 995-1015.
68. Wierenga, R. K., Noble, M. E. M., & Davenport, R. C. (1992) J. Mol. Biol. 224, 1115-1126.
69. Zhang, X. J., Baase, W. A., & Matthews, B. W. (1991) Biochemistry 30, 2012-2017.