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Physiological Reviews, Vol. 79, No. 2, April 1999, pp. 425-449
Copyright ©1999 by the American Physiological Society
Department of Chemistry and Biochemistry, The University of California, Santa Cruz, California
Fink, Anthony L.
The folding of most newly
synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules
recognize and bind to nascent polypeptide chains and partially folded
intermediates of proteins, preventing their aggregation and misfolding.
There are several families of chaperones; those most involved in
protein folding are the 40-kDa heat shock protein (HSP40; DnaJ), 60-kDa heat shock protein (HSP60; GroEL), and 70-kDa heat shock protein (HSP70; DnaK) families. The availability of high-resolution
structures has facilitated a more detailed understanding of the complex
chaperone machinery and mechanisms, including the ATP-dependent
reaction cycles of the GroEL and HSP70 chaperones. For both of these
chaperones, the binding of ATP triggers a critical conformational
change leading to release of the bound substrate protein. Whereas the
main role of the HSP70/HSP40 chaperone system is to minimize
aggregation of newly synthesized proteins, the HSP60 chaperones also
facilitate the actual folding process by providing a secluded
environment for individual folding molecules and may also promote the
unfolding and refolding of misfolded intermediates.
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B. A. Buckley and G. E. Hofmann Thermal acclimation changes DNA-binding activity of heat shock factor 1 (HSF1) in the goby Gillichthys mirabilis: implications for plasticity in the heat-shock response in natural populations J. Exp. Biol., October 15, 2002; 205(20): 3231 - 3240. [Abstract] [Full Text] [PDF]
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R. K. Thimmulappa, K. H. Mai, S. Srisuma, T. W. Kensler, M. Yamamoto, and S. Biswal Identification of Nrf2-regulated Genes Induced by the Chemopreventive Agent Sulforaphane by Oligonucleotide Microarray Cancer Res., September 15, 2002; 62(18): 5196 - 5203. [Abstract] [Full Text] [PDF]
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S. Roth, N. Willcox, R. Rzepka, M. P. Mayer, and I. Melchers Major Differences in Antigen-Processing Correlate with a Single Arg71{leftrightarrow}Lys Substitution in HLA-DR Molecules Predisposing to Rheumatoid Arthritis and with Their Selective Interactions with 70-kDa Heat Shock Protein Chaperones J. Immunol., September 15, 2002; 169(6): 3015 - 3020. [Abstract] [Full Text] [PDF]
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 C. A. Christensen, S. W. Gorsich, R. H. Brown, L. G. Jones, J. Brown, J. M. Shaw, and G. N. Drews Mitochondrial GFA2 Is Required for Synergid Cell Death in Arabidopsis PLANT CELL, September 1, 2002; 14(9): 2215 - 2232. [Abstract] [Full Text] [PDF]
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A. N. Boone and M. M. Vijayan Glucocorticoid-mediated attenuation of the hsp70 response in trout hepatocytes involves the proteasome Am J Physiol Regulatory Integrative Comp Physiol, September 1, 2002; 283(3): R680 - R687. [Abstract] [Full Text] [PDF]
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H. Zhang, K. W. Peters, F. Sun, C. R. Marino, J. Lang, R. D. Burgoyne, and R. A. Frizzell Cysteine String Protein Interacts with and Modulates the Maturation of the Cystic Fibrosis Transmembrane Conductance Regulator J. Biol. Chem., August 2, 2002; 277(32): 28948 - 28958. [Abstract] [Full Text] [PDF]
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G. E. Hofmann, B. A. Buckley, S. P. Place, and M. L. Zippay Molecular Chaperones in Ectothermic Marine Animals: Biochemical Function and Gene Expression Integr. Comp. Biol., August 1, 2002; 42(4): 808 - 814. [Abstract] [Full Text] [PDF]
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P. M. Halpin, C. J. Sorte, G. E. Hofmann, and B. A. Menge Patterns of Variation in Levels of Hsp70 in Natural Rocky Shore Populations from Microscales to Mesoscales Integr. Comp. Biol., August 1, 2002; 42(4): 815 - 824. [Abstract] [Full Text] [PDF]
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 J C Ranford and B Henderson Chaperonins in disease: mechanisms, models, and treatments Mol. Pathol., August 1, 2002; 55(4): 209 - 213. [Abstract] [Full Text] [PDF]
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Y. Yamauchi, K. Wada, F. Goshima, T. Daikoku, K. Ohtsuka, and Y. Nishiyama Herpes simplex virus type 2 UL14 gene product has heat shock protein (HSP)-like functions J. Cell Sci., June 15, 2002; 115(12): 2517 - 2527. [Abstract] [Full Text] [PDF]
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 C.-C. Chang, C.-T. Tsai, and C.-Y. Chang Structural restoration of inactive recombinant fish growth hormones by chemical chaperonin and solvent restraint approaches Protein Eng. Des. Sel., May 1, 2002; 15(5): 437 - 441. [Abstract] [Full Text] [PDF]
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S. H. H. Chan, K.-F. Chang, C.-C. Ou, and J. Y. H. Chan Up-Regulation of Glutamate Receptors in Nucleus Tractus Solitarii Underlies Potentiation of Baroreceptor Reflex by Heat Shock Protein 70 Mol. Pharmacol., May 1, 2002; 61(5): 1097 - 1104. [Abstract] [Full Text] [PDF]
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 M. Noda, J.C. Wataha, M. Kaga, P.E. Lockwood, K.R. Volkmann, and H. Sano Components of Dentinal Adhesives Modulate Heat Shock Protein 72 Expression in Heat-stressed THP-1 Human Monocytes at Sublethal Concentrations Journal of Dental Research, April 1, 2002; 81(4): 265 - 269. [Abstract] [Full Text] [PDF]
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 I. Kurucz, A. Morva, A. Vaag, K.-F. Eriksson, X. Huang, L. Groop, and L. Koranyi Decreased Expression of Heat Shock Protein 72 In Skeletal Muscle of Patients With Type 2 Diabetes Correlates With Insulin Resistance Diabetes, April 1, 2002; 51(4): 1102 - 1109. [Abstract] [Full Text] [PDF]
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Y. P. Bao, L. J. Cook, D. O'Donovan, E. Uyama, and D. C. Rubinsztein Mammalian, Yeast, Bacterial, and Chemical Chaperones Reduce Aggregate Formation and Death in a Cell Model of Oculopharyngeal Muscular Dystrophy J. Biol. Chem., March 29, 2002; 277(14): 12263 - 12269. [Abstract] [Full Text] [PDF]
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B. A. Buckley, M.-E. Owen, and G. E. Hofmann Adjusting the thermostat: the threshold induction temperature for the heat-shock response in intertidal mussels (genus Mytilus) changes as a function of thermal history J. Exp. Biol., March 12, 2002; 204(20): 3571 - 3579. [Abstract] [Full Text] [PDF]
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C. K. Bailey, I. F. M. Andriola, H. H. Kampinga, and D. E. Merry Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy Hum. Mol. Genet., March 1, 2002; 11(5): 515 - 523. [Abstract] [Full Text] [PDF]
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H. O. Barazi, L. Zhou, N. S. Templeton, H. C. Krutzsch, and D. D. Roberts Identification of Heat Shock Protein 60 as a Molecular Mediator of {alpha}3{beta}1 Integrin Activation Cancer Res., March 1, 2002; 62(5): 1541 - 1548. [Abstract] [Full Text] [PDF]
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J.-J. Hung, C.-S. Chung, and W. Chang Molecular Chaperone Hsp90 Is Important for Vaccinia Virus Growth in Cells J. Virol., February 1, 2002; 76(3): 1379 - 1390. [Abstract] [Full Text] [PDF]
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 A. Kimura, T. Hamada, E. H. Morita, and H. Hayashi A High Temperature-Sensitive Mutant of Synechococcus sp. PCC 7002 with Modifications in the Endogenous Plasmid, pAQ1 Plant Cell Physiol., February 1, 2002; 43(2): 217 - 223. [Abstract] [Full Text] [PDF]
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 K.-C. Yeh, M. C. Peck, and S. R. Long Luteolin and GroESL Modulate In Vitro Activity of NodD J. Bacteriol., January 15, 2002; 184(2): 525 - 530. [Abstract] [Full Text] [PDF]
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C. Habich, K. Baumgart, H. Kolb, and V. Burkart The Receptor for Heat Shock Protein 60 on Macrophages Is Saturable, Specific, and Distinct from Receptors for Other Heat Shock Proteins J. Immunol., January 15, 2002; 168(2): 569 - 576. [Abstract] [Full Text] [PDF]
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H. Zhou, S.-H. Li, and X.-J. Li Chaperone Suppression of Cellular Toxicity of Huntingtin Is Independent of Polyglutamine Aggregation J. Biol. Chem., December 14, 2001; 276(51): 48417 - 48424. [Abstract] [Full Text] [PDF]
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M. W. Ribbe and B. K. Burgess The chaperone GroEL is required for the final assembly of the molybdenum-iron protein of nitrogenase PNAS, April 25, 2001; (2001) 101119498. [Abstract] [Full Text]
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S. P. Place and G. E. Hofmann Temperature interactions of the molecular chaperone Hsc70 from the eurythermal marine goby Gillichthys mirabilis J. Exp. Biol., January 8, 2001; 204(15): 2675 - 2682. [Abstract] [Full Text] [PDF]
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H. Smidt, M. van Leest, J. van der Oost, and W. M. de Vos Transcriptional Regulation of the cpr Gene Cluster in ortho-Chlorophenol-Respiring Desulfitobacterium dehalogenans J. Bacteriol., October 15, 2000; 182(20): 5683 - 5691. [Abstract] [Full Text]
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F.-X. Beck, W. Neuhofer, and E. Muller Molecular chaperones in the kidney: distribution, putative roles, and regulation Am J Physiol Renal Physiol, August 1, 2000; 279(2): F203 - F215. [Abstract] [Full Text] [PDF]
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