Structure, function, and temperature sensitivity of directed, random mutants at proline 76 and glycine 77 in Ω-Loop D of yeast iso-1-cytochrome c

Biochemistry

Volumn 37, Issue 8, 1998, Pages 2477-2487

  Fetrow, Jacquelyn S ^a   Spitzer, Jennifer S ^a   Gilden, Brad M ^a   Mellender, Scott J ^a   Begley, Thomas J ^a   Haas, Brian J ^a   Boose, Terry L ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; GLYCINE; PROLINE;

ARTICLE; BINDING KINETICS; CIRCULAR DICHROISM; ENTROPY; ENZYME ANALYSIS; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; STRUCTURE ACTIVITY RELATION; TEMPERATURE SENSITIVITY;

ANIMALS; BINDING SITES; CIRCULAR DICHROISM; CYTOCHROME C GROUP; CYTOCHROMES C; EUKARYOTIC CELLS; GLYCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROLINE; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TEMPERATURE;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 0032562144     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972279a     Document Type: Article

References (97)

1. Leszczynski, J. F., and Rose, G. D. (1986) Science 234, 849-855.
2. Ptitsyn, O. B. (1981) FEBS Lett. 131, 197-201.
3. Wright, P. E., Dyson, H. J., and Lerner, R. A. (1988) Biochemistry 27, 7167-7175.
4. Predki, P. F., Agrawal, V., Brünger, A. T., and Regan, L. (1996) Nat. Struct. Biol. 3, 54-58.
5. Fetrow, J. S., Horner, S. R., Oehrl, W., Schaak, D. L., Boose, T. L., and Burton, R. E. (1997) Protein Sci. 6, 195-208.
6. Zhou, H. X., Hoes, R. H., and DeGrado, W. F. (1996) Nat. Struct. Biol. 3, 446-451.
7. Venkatachalam, C. M. (1968) Biopolymers 6, 1425-1436.
8. Lewis, P. N., Momany, F. A., and Scheraga, H. A. (1973) Biochim. Biophys. Acta 303, 211-229.
9. Richardson, J. S. (1981) Adv. Protein Chem. 34, 167-339.
10. Rose, G. D., Gierasch, L. M., and Smith, J. A. (1985) Adv. Protein Chem. 37, 1-109.
11. Chou, P. Y., and Fasman, G. D. (1977) J. Mol. Biol. 115, 135-175.
12. Wilmot, C. M., and Thornton, J. M. (1990) Protein Eng. 3, 479-493.
13. Hutchinson, E. G., and Thornton, J. M. (1994) Protein Sci. 3, 2207-2216.
14. Milner-White, E. J., and Poet, R. (1986) Biochem. J. 240, 289-292.
15. Sibanda, B. L., and Thornton, J. M. (1985) Nature 316, 170-174.
16. Sibanda, B. L., Blundell, T. L., and Thornton, J. M. (1989) J. Mol. Biol. 206, 759-778.
17. Efimov, A. V. (1991) Protein Eng. 4, 245-250.
18. Wintjens, R. T., Rooman, M. J., and Wodak, S. J. (1996) J. Mol. Biol. 255, 235-253.
19. Brunet, A. P., Huang, E. S., Huffine, M. E., Loeb, J. E., Weltman, R. J., and Hecht, M. H. (1993) Nature 364, 355-358.
20. Predki, P. F., and Regan, L. (1995) Biochemistry 34, 9834-9839.
21. Chou, K.-C., Maggiora, G. M., and Scheraga, H. A. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 7315-7319.
22. Hynes, T. R., Kautz, R. A., Goodman, M. A., Gill, J. F., and Fox, R. O. (1989) Nature 339, 73-76.
23. Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A., and Wright, P. E. (1988) J. Mol. Biol. 201, 161-200.
24. Milburn, P. J., Konishi, Y., Meinwald, Y. C., and Scheraga, H. A. (1987) J. Am. Chem. Soc. 109, 4486-4496.
25. Shin, H.-C., Merutka, G., Waltho, J. P., Wright, P. E., and Dyson, H. J. (1993) Biochemistry 32, 6348-6355.
26. Chothia, C., and Lesk, A. M. (1987) J. Mol. Biol. 196, 901-917.
27. Tramontano, A., Chothia, C., and Lesk, A. M. (1989) Proteins: Struct., Funct., Genet. 6, 382-394.
28. Tramontano, A., and Lesk, A. M. (1992) Proteins: Struct., Funct., Genet. 13, 231-245.
29. Urfer, R., and Kirschner, K. (1992) Protein Sci. 1, 31-45.
30. Scheerlinck, J.-P. Y., Lasters, I., Claessens, M., DeMaeyer, M., Pio, F., Delhaise, P., and Wodak, S. J. (1992) Proteins: Struct., Funct., Genet. 12, 299-313.
31. Edwards, M., Sternberg, M., and Thornton, J. (1987) Protein Eng. 1, 173-181.
32. Ring, C. S., Kneller, D. G., Langridge, R., and Cohen, F. E. (1992) J. Mol. Biol. 224, 685-699.
33. Fetrow, J. S. (1995) FASEB J. 9, 708-717.
34. Kwasigroch, J.-M., Chomilier, J., and Mornon, J.-P. (1996) J. Mol. Biol. 259, 855-872.
35. Donate, L. E., Rufino, S. D., Canard, L. H. J., and Blundell, T. L. (1996) Protein Sci. 5, 2600-2616.
36. Oliva, B., Bates, P. A., Querol, E., Avilés, F. X., and Sternberg, M. J. E. (1997) J. Mol. Biol. 266, 814-830.
37. Mulligan-Pullyblank, P., Spitzer, J. S., Gilden, B. M., and Fetrow, J. S. (1996) J. Biol. Chem. 271, 8633-8645.
38. Sherman, F., Stewart, J. W., Parker, J. H., Inhaber, E., Shipman, N. A., Putterman, G. J., Gardishy, R. L., and Margoliash, E. (1968) J. Biol. Chem. 243, 5446-5456.
39. Sherman, F., Stewart, J. W., Jackson, M., Gilmore, R. A., and Parker, J. H. (1974) Genetics 77, 255-284.
40. Hampsey, D. M., Das, G., and Sherman, F. (1986) J. Biol. Chem. 261, 3259-3271.
41. Auld, D. S., and Pielak, G. J. (1991) Biochemistry 30, 8684-8690.
42. Fredericks, Z. L., and Pielak, G. J. (1993) Biochemistry 32, 929-936.
43. Louie, G. V., and Brayer, G. D. (1990) J. Mol. Biol. 214, 527-555.
44. Berghuis, A. M., and Brayer, G. D. (1992) J. Mol. Biol. 223, 959-976.
45. Murphy, M. E. P., Nall, B. T., and Brayer, G. D. (1992) J. Mol. Biol. 227, 160-176.
46. Bushnell, G. W., Louie, G. V., and Brayer, G. D. (1990) J. Mol. Biol. 214, 585-595.
47. Takano, T., and Dickerson, R. E. (1981) J. Mol. Biol. 153, 79-94.
48. Takano, T., and Dickerson, R. E. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6371-6375.
49. Ochi, H., Hata, V., Tanaka, N., Kakudo, M., Sakurai, T., Aihara, S., and Morita, Y. (1983) J. Mol. Biol. 166, 407-418.
50. Tanaka, N., Yamane, T., Tsukihara, T., Ashida, T., and Kakudo, M. (1975) J. Biochem. (Tokyo) 77, 147.
51. Qi, P. X., DiStefano, D. L., and Wand, A. J. (1994) Biochemistry 33, 6408-6417.
52. Qi, P. X., Beckman, R. A., and Wand, A. J. (1996) Biochemistry 35, 12275-12286.
53. Banci, L., Bertini, I., Gray, H. B., Luchinat, C., Reddig, T., Rosato, A., and Turano, P. (1997) Biochemistry 36, 9867-9877.
54. Baistrocchi, P., Banci, L., Vertini, I., Turano, P., Bren, K. L., and Gray, H. B. (1996) Biochemistry 35, 13788-13796.
55. Banci, L., Bertini, I., Bren, K. L., Gray, H. B., Sompornpisut, P., and Turano, P. (1997) Biochemistry 36, 8992-9001.
56. Berghuis, A. M., Guillemette, J. G., McLendon, G., Sherman, F., Smith, M., and Brayer, G. D. (1994) J. Mol. Biol. 236, 786-799.
57. Berghuis, A. M., Guillemette, J. G., Smith, M., and Brayer, G. D. (1994) J. Mol. Biol. 235, 1326-1341.
58. Lo, T. P., Murphy, M. E. P., Guillemette, J. G., Smith, M., and Brayer, G. D. (1995) Protein Sci. 4, 198-208.
59. Lo, T. P., Guillemette, J. G., Louie, G. V., Smith, M., and Brayer, G. D. (1995) Biochemistry 34, 163-171.
60. Louie, G. V., Pielak, G. J., Smith, M., and Brayer, G. D. (1988) Biochemistry 27, 7870-7876.
61. Louie, G. V., and Brayer, B. D. (1989) J. Mol. Biol. 210, 313-322.
62. Murphy, M. E. P., Fetrow, J. S., Burton, R. E., and Brayer, G. D. (1993) Protein Sci. 2, 1429-1440.
63. Chau, M.-H., Cai, M. L., and Timkovich, R. (1990) Biochemistry 29, 5076-5087.
64. Gao, Y., Boyd, J., Williams, R. J. P., and Pielak, G. J. (1990) Biochemistry 29, 6994-7003.
65. Gao, Y., Boyd, J., Pielak, G. J., and Williams, R. J. P. (1991) Biochemistry 30, 1928-1934.
66. Hong, X., and Dixon, D. W. (1989) FEBS Lett. 246, 105-108.
67. Marmorino, J. L., Auld, D. S., Betz, S. F., Doyle, D. F., Young, G. B., and Pielak, G. J. (1993) Protein Sci. 2, 1966-1974.
68. Pielak, G. J., Boyd, J., Moore, G. R., and Williams, R. J. P. (1988) Eur. J. Biochem. 177, 167-177.
69. Baxter, S. M., Boose, T. L., and Fetrow, J. S. (1997) J. Am. Chem. Soc. 119, 9899-9900.
70. Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Science 269, 192-197.
71. Bai, Y., and Englander, S. W. (1996) Proteins: Struct., Funct., Genet. 24, 145-151.
72. Roder, H., Elove, G. A., and Englander, S. W. (1988) Nature 335, 700-704.
73. Colón, W., Elöve, G. A., Wakem, L. P., Sherman, F., and Roder, H. (1996) Biochemistry 35, 5538-5549.
74. Elöve, G. A., Bhuyan, A. K., and Roder, H. (1994) Biochemistry 33, 6925-6935.
75. Qu, K., Vaughn, J. L., Sienkiewicz, A., Scholes, C. P., and Fetrow, J. S. (1997) Biochemistry 36, 2884-2897.
76. Pierce, M. M., and Nail, B. T. (1997) Protein Sci. 6, 618-627.
77. Pettigrew, G. W., and Moore, G. R. (1987) Cytochromes c Biological Aspects, Springer-Verlag, Berlin.
78. Pielak, G. J., Auld, D. S., Beasley, J. R., Betz, S. F., Cohen, D. S., Doyle, D. F., Finger, S. A., Fredericks, Z. L., Hilgen-Willis, S., Saunders, A. J., and Trojak, S. K. (1995) Biochemistry 34, 3268-3276.
79. Fumo, G., Spitzer, J. S., and Fetrow, J. S. (1995) Gene 164, 33-39.
80. Fetrow, J. S., Cardillo, T. S., and Sherman, F. (1989) Proteins: Struct., Funct., Genet. 6, 372-381.
81. Cutler, R. L., Pielak, G. J., Mauk, A. G., and Smith, M. (1987) Protein Eng. 1, 95-99.
82. Schweingruber, M. E., Sherman, F., and Stewart, J. W. (1977) J. Biol. Chem. 252, 6577-6580.
83. Sherman, F., and Slonimski, P. P. (1964) Biochim. Biophys. Acta 90, 1-15.
84. Cottrell, S. F., Rabinowitz, M., and Getz, G. S. (1975) J. Biol. Chem. 250, 4087-4094.
85. Linske-O'Connell, L. I., Sherman, F., and McLendon, G. (1995) Biochemistry 34, 7094-7102.
86. Schagger, H., and von Jagow, G. (1987) Anal. Biochem. 166, 368-379.
87. Margoliash, E., and Frohwirt, N. (1959) Biochem. J. 71, 570-572.
88. Strickland, E. H. (1974) CRC Crit. Rev. Biochem. 2, 113-174.
89. Elwell, M. L., and Schellman, J. A. (1977) Biochim. Biophys. Acta 494, 367-383.
90. Cohen, D. S., and Pielak, G. J. (1994) Protein Sci. 3, 1253-1260.
91. Moore, G. R., and Pettigrew, G. W. (1990) Cytochromes c. Evolutionary, Structural and Physicochemical Aspects, Springer-Verlag: Berlin.
92. Schweingruber, M. E., Stewart, J. W., and Sherman, F. (1979) J. Biol. Chem. 254, 4132-4143.
93. Ernst, J. F., Hampsey, D. M., Stewart, J. W., Rackovsky, S., Goldstein, D., and Sherman, F. (1985) J. Biol. Chem. 260, 13225-13236.
94. Luntz, T. L., Schejter, A., Barber, E. A. E., and Margoliash, E. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 3524-3528.
95. Lee, B., and Richards, F. M. (1971) J. Mol. Biol. 55, 379-400.
96. Pelletier, H., and Kraut, J. (1992) Science 258, 1748-1755.
97. Appleby, C. A., and Morton, R. K. (1954) Nature (London) 173, 749-752.