Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides

Journal of Biological Chemistry

Volumn 272, Issue 39, 1997, Pages 24646-24666

  Leroux, Michel R ^a   Melki, Ronald ^b   Gordon, Bruce ^a   Batelier, Gérard ^b   Candido, E Peter M ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; POLYPEPTIDE; TUBULIN;

ARTICLE; CAENORHABDITIS ELEGANS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BIOPOLYMERS; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CITRATE (SI)-SYNTHASE; HEAT-SHOCK PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RABBITS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TUBULIN;

CAENORHABDITIS ELEGANS;

EID: 0030826325     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.39.24646     Document Type: Article

References (105)

1. Gething, M. J., and Sambrook, J. (1992) Nature 355, 33-45
2. Hendrick, J. P., and Hartl, F.-U. (1993) Annu. Rev. Biochem. 62, 349-384
3. Parsell, D. A., and Lindquist, S. (1994) in The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R. I., Tissières, A., and Georgopoulos, C., eds) pp. 457-494, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
4. Buchner, J. (1996) FASEB J. 10, 10-19
5. Hartl, F.-U. (1996) Nature 381, 571-580
6. Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K., and Hartl, F.-U. (1992) Nature 356, 683-689
7. Frydman, J., and Hartl, F.-U. (1996) Science 272, 1497-1502
8. Sanchez, Y., and Lindquist, S. L. (1990) Science 248, 1112-1115
9. Sanchez, Y., Taulien, J., Borkovich, K. A., and Lindquist, S. (1992) EMBO J. 11, 2357-2364
10. Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994) Nature 372, 475-478
11. Feder, M. E., Cartano, N. V., Milos, L., Krebs, R. A., and Lindquist, S. L. (1996) J. Exp. Biol. 199, 1837-1844
12. Landry, J., Chretien, P., Lambert, H., Hickey, E., and Weber, L. A. (1989) J. Cell Biol. 109, 7-15
13. Lavoie, J. N., Gingras-Breton, G., Tanguay, R. M., and Landry, J. (1993) J. Biol. Chem. 268, 3420-3429
14. Yen, K. W., Jinn, T. L., Yeh, C. H., Chen, Y. M., and Lin, C. Y. (1994) Biotech. Appl. Biochem. 19, 41-49
15. Arrigo, A.-P., and Landry, J. (1994) in The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R. I., Tissières, A., and Georgopoulos, C., eds) pp. 335-373, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
16. Caspers, G.-J., Leunissen, J. A. M., and De Jong, W. W. (1995) J. Mol. Evol. 40, 238-248
17. Bult, C. J., White, O., Olsen, G. J., Zhou, L., Fleischmann, R. D., Sutton, G. G., Blake, J. A., FitzGerald, L. M., Clayton, R. A., Gocayne, J. D., Kerlavage, A. R., Dougherty, B. A., Tomb, J.-F., Adams, M. D., Reich, C. I., Overbeek, R., Kirkness, E. F., Weinstock, K. G., Merrick, J. M., Glodek, A., Scott, J. L., Geoghagen, N. S. M., Weidman, J. F., Fuhrmann, J. L., Nguyen, D., Utterback, T. R., Kelley, J. M., Peterson, J. D., Sadow, P. W., Hanna, M. C., Cotton, M. D., Roberts, K. M., Hurst, M. A., Kaine, B. P., Borodovsky, M., Klenk, H.-P., Fraser, C. M., Smith, H. O., Woese, C. R., and Venter, J. C. (1996) Science 273, 1058-1073
18. Ingolia, T. D., and Craig, E. A. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 2360-2364
19. Russnak, R. H., Jones, D., and Candido, E. P. M. (1983) Nucleic Acids Res. 11, 3187-3205
20. Wistow, G. (1985) FEBS Lett. 181, 1-6
21. King, C. R., and Piatigorski, J. (1983) Cell 32, 707-712
22. Russnak, R. H., and Candido, E. P. M. (1985) Mol. Cell. Biol. 5, 1268-1278
23. Van den Oetelaar, P. J., and Hoender, H. J. (1989) Biochim. Biophys. Acta 995, 91-96
24. Carver, J. A., Aquilina, J. A., and Truscott, R. J. (1993) Biochim. Biophys. Acta 1164, 22-28
25. Siezen, R. J., and Argos, P. (1983) Biochim. Biophys. Acta 748, 55-67
26. Merck, K. B., Groenen, P. J. T. A., Voorter, C. E. M., de Haard-Hoekman, W. A., Horwitz, J., Bloemendal, H., and de Jong, W. W. (1993a) J. Biol. Chem. 268, 1046-1052
27. Carver, J. A., Aquilina, J. A., Truscott, R. J., and Ralston, G. B. (1992) FEBS Lett. 311, 143-149
28. Carver, J. A., Esposito, G., Schwedersky, G., and Gaestel, M. (1995a) FEBS Lett. 369, 305-310
29. Groenen, P. J. T. A., Merck, K. B., de Jong, W. W., and Bloemendal, H. (1994) Eur. J. Biochem. 225, 1-19
30. Chang, Z., Primm, T. P., Jakana, J., Lee, I. H., Serysheva, I., Chiu, W., Gilbert, H. F., and Quiocho, F. A. (1996) J. Biol. Chem. 271, 7218-7223
31. Waters, E. R., Lee, G. J., and Vierling, E. (1996) J. Exp. Bot. 47, 325-338
32. Bentley, N. J., Fitch, I. T., and Tuite, M. F. (1992) Yeast 8, 95-106
33. Horwitz, J. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 10449-10453
34. Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993) J. Biol. Chem. 268, 1517-1520
35. Lee, G. J., Pokala, N., and Vierling, E. (1995) J. Biol. Chem. 270, 10432-10438
36. Welch, W. J., and Suhan, J. P. (1985) J. Cell Biol. 101, 1198-1211
37. Chiesi, M., Longoni, S., and Limbruno, U. (1990) Mol. Cell. Biochem. 97, 129-136
38. Bennardini, F., Wrzosek, A., and Chiesi, M. (1992) Circ. Res. 71, 288-294
39. Gopalakrishnan, S., and Takemoto, L. (1992) Curr. Eye Res. 11, 929-933
40. Nicholl, I. D., and Quintan, R. A. (1994) EMBO J. 13, 945-953
41. Lavoie, J. N., Hickey, E., Weber, L. A., and Landry, J. (1993) J. Biol. Chem. 268, 24210-24214
42. Landry, J., and Huot, J. (1995) Biochem. Cell Biol. 73, 703-707
43. Lavoie, J. N., Lambert, H., Hickey, E., Weber, L. A., and Landry, J. (1995) Mol. Cell Biol. 15, 505-516
44. Huot, J., Houle, F., Spitz, D. R., and Landry, J. (1996) Cancer Res. 56, 273-279
45. Wang, K., and Spector, A. (1996) Eur. J. Biochem. 242, 55-66
46. Dixon, D. K., Jones, D., and Candido, E. P. M. (1990) DNA Cell Biol. 9, 177-191
47. Stringham, E. G., Dixon, D. K., Jones, D., and Candido, E. P. M. (1992) Mol. Biol. Cell 3, 221-233
48. Jones, D., Russnak, R. H., Kay, R. J., and Candido, E. P. M. (1986) J. Biol. Chem. 261, 12006-12015
49. Candido, E. P. M., Jones, D., Dixon, D. K., Graham, R. W., Russnak, R. H., and Kay, R. J. (1989) Genome 31, 690-697
50. Jones, D., Stringham, E. G., Babich, S. L., and Candido, E. P. M. (1996) Toxicology 109, 199-127
51. Leroux, M. R., Ma, B. J., Batelier, G., Melki, R., and Candido, E. P. M. (1997) J. Biol. Chem. 272, 12847-12853
52. Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Methods Enzymol. 185, 60-89
53. Stafford, W. F., III (1992) Anal. Biochem. 203, 295-301
54. Philo, J. S. (1994) in Modern Analytical Ultracentrifugation: Acquisition and Interpretation of Data for Biological and Synthetic Polymer Systems (Schuster, T. M., and Laue, T. M., eds) pp. 156-170, Birkhauser, Boston
55. Kuntz, I. D. (1971) J. Am. Chem. Soc. 93, 514-516
56. Laue, T. M., Shah, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) in Analytical Ultracentrifugation in Biochemistry and Polymer Sciences (Harding, S. E., Rowe, A. J., and Horton, J. C., eds) pp. 90-125, The Royal Society of Chemistry, Cambridge, United Kingdom
57. Lin, T.-H., Quinn, T., Walsh, M., Grandgenett, D., and Lee, J. C. (1991) J. Biol. Chem. 266, 1635-1640
58. Melki, R., and Cowan, N. J. (1994) Mol. Cell. Biol. 14, 2895-2904
59. Spudich, J. A., and Watt, S. (1971) J. Biol. Chem. 246, 4866-4871
60. Eisenberg, E., and Kielley, W. W. (1974), J. Biol. Chem. 249, 4742-4748
61. McLean-Fletcher, S., and Pollard, T. D. (1980) Biochem. Biophys. Res. Commun. 96, 18-27
62. Kouyama, T., and Mihashi, K. (1981) Eur. J. Biochem. 114, 33-38
63. Detmers, P., Weber, A., Elzinga, M., and Stephens, R. E. (1981) J. Biol. Chem. 256, 99-105
64. Shelanski, M. L., Gaskin, F., and Cantor, C. R. (1973) Proc. Natl. Acad. Sci. U. S. A. 70, 765-768
65. Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., and Kirschner, M. W. (1975) Proc. Natl. Acad. Sci. U. S. A. 72, 1858-1862
66. Mejillano, M. R., and Himes, R. H. (1989) Biochemistry 28, 6518-6524
67. Singh, M., Brooks, G. C., and Srere, P. A. (1970) J. Biol. Chem. 245, 4636-4640
68. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
69. Gordon, D. G., Yang, Y. Z., and Korn, E. D. (1976) J. Biol. Chem. 251, 7474-7479
70. Krauhs, E., Little, M., Kempf, T., Hofer-Warbinek, R., Ade, W., and Ponstingl, H. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 4156-4160
71. Hockertz, M. K., Clark-Lewis, I., and Candido, E. P. M. (1991) FEBS Lett. 280, 375-378
72. Zhi, W., Landry, S. J., Gierasch, L. M., and Srere, P. A. (1992) Protein Sci. 1, 522-529
73. Wiech, H., Buchner, J., Zimmermann, R., and Jakob, U. (1992) Nature 358, 169-170
74. Jakob, U., Lilie, H., Meyer, I., and Buchner, J. (1995) J. Biol. Chem. 270, 7288-7294
75. Bose, S., Weikl, T., Bügl, H., and Buchner, J. (1996) Science 274, 1715-1717
76. Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F. X., and Kiefhaber, T. (1991) Biochemistry 30, 1586-1591
77. Wang, K., and Spector, A. (1994) J. Biol. Chem. 269, 13601-13608
78. Staros, J. V. (1982) Biochemistry 21, 3950-3955
79. Merck, K. B., De Haard-Hoekman, W. A., Oude Essink, B. B., Bloemendal, H., and De Jong, W. W. (1992) Biochim. Biophys. Acta 1130, 267-276
80. Merck, K. B., Horwitz, J., Kersten, M., Overkamp, P., Gaestel, M., Bloemendal, H., and De Jong, W. W. (1993) Mol. Biol. Rep. 18, 209-215
81. Smulders, R. H. P. H., Merck, K. B., Aendekerk, J., Horwitz, J., Takemoto, L., Slingsby, C., Bloemendal, H., and De jong, W. W. (1995) Eur. J. Biochem. 232, 834-838
82. Smulders, R. H. P. H., Carver, J. A., Lindner, R. A., van Boekel, M. A. M., Bloemendal, H., and de Jong, W. W. (1996) J. Biol. Chem. 271, 29060-29066
83. Plater, M. L., Goode, D., and Crabbe, M. J. C. (1996) J. Biol. Chem. 271, 28558-28566
84. Kato, K., Hasegawa, K., Goto, S., and Inaguma, Y. (1994) J. Biol. Chem. 269, 11274-11278
85. Smulders, R. H. P. H., van Geel, I. G., Gerards, W. L. H., Bloemendal, H., and de Jong, W. W. (1995) J. Biol. Chem. 270, 13916-13924
86. Siezen, R. J., Bindels, J. G., and Hoenders, H. J. (1980) Eur. J. Biochem. 107, 243-249
87. Gesierich, U., and Pfeil, W. (1996) FEBS Lett. 393, 151-154
88. Martin, J., Horwich, A. L., and Hartl, F.-U. (1992) Science 258, 995-998
89. Freeman, B. C., and Morimoto, R. I. (1996) EMBO J. 15, 2969-2979
90. Carver, J. A., Guerreiro, N., Nicholls, K. A., and Truscott, R. J. W. (1995b) Biochim. Biophys. Acta 1252, 251-260
91. Das, K. P., Petrash, J. M., and Surewicz, W. K. (1996) J. Biol. Chem. 271, 10449-10452
92. Rajaraman, K., Raman, B., and Rao, Ch. M. (1996) J. Biol. Chem. 271, 27595-27600
93. Carver, J. A., Aquilina, J. A., Cooper, P. G., Williams, G. A., and Truscott, R. J. W. (1994) Biochim. Biophys. Acta 1204, 195-206
94. Farahbakhsh, Z. T., Huang, Q.-L., Ding, L.-L., Altenbach, C., Steinhoff, H.-J., Horwitz, J., and Hubbell, W. L. (1995) Biochemistry 34, 509-516
95. Lee, G. J., Roseman, A. M., Saibil, H. R., and Vierling, E. (1997) EMBO J. 16, 659-671
96. Singh, K., Groth-Vasselli, B., Kumosinski, T. F., and Farnsworth, P. N. (1995) FEBS Lett. 372, 283-287
97. Schirmer, E. C., Glover, J. R., Singer, M. A., and Lindquist, S. (1996) Trends Biochem. Sci. 21, 289-296
98. Longoni, S., Lattonen, S., Bullock, G., and Chiesi, M. (1990) Mol. Cell. Biochem. 97, 121-128
99. Augusteyn, R. C., and Koretz, J. F. (1987) FEBS Lett. 222, 1-5
100. Linder, B., Jin, Z., Freedman, J. H., and Rubin, C. S. (1996) J. Biol. Chem. 271, 30158-30166
101. Melki, R., Rommelaere, H., Leguy, R., Vandekerckhove, J., and Ampe, C. (1996) Biochemistry 35, 10422-10435
102. Freeman, B. C., Toft, D. O., and Morimoto, R. I. (1996) Science 274, 1718-1720
103. Straus, D. B., Walter, W. A., and Gross, C. A. (1988) Genes Dev. 2, 1851-1858
104. Hayes, S. A., and Dice, J. F. (1996) J. Cell Biol. 132 255-258
105. Ehrnsperger, M., Gräber, S., Gaestel, M., and Buchner, J. (1997) EMBO J. 16, 221-229