The role of molecular chaperones in mitochondrial protein import and folding

International Review of Cytology

Volumn 174, Issue , 1997, Pages 127-193

  Ryan, Michael T ^a,b   Naylor, Dean J ^a   Høj, Peter B ^a   Clark, Margaret S ^a   Hoogenraad, Nicholas J ^a  

^a LA TROBE UNIVERSITY   (Australia)

^b UNIVERSITY OF ADELAIDE   (Australia)

Author keywords

Heat shock; Mitochondria; Molecular chaperone; Protein folding; Protein import; Proteolysis

Indexed keywords

CELL PROTEIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN 70; PROTEINASE;

ATHEROSCLEROSIS; AUTOIMMUNITY; ESCHERICHIA COLI; GENE ACTIVATION; GENE EXPRESSION REGULATION; HUMAN; IMMUNE RESPONSE; INFECTION; MEMBRANE TRANSPORT; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN TRANSPORT; REVIEW; STRESS; SYMBIOSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA;

EID: 0030927540     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)62117-8     Document Type: Review

References (370)

1. Abravaya, K., Myers, M. P., Murphy, S. P., and Morimoto, R. I. (1992). The human heat shock protein hsp70 interacts with HSF, the transcription factor which regulates heat shock gene transcription. Genes Dev. 6,1153-1164.
2. Adams, M. D., Dubnick, M., Kerlavage, A. R., Moreno, R., Kelley, J. M., Utterback, T. R., Nagle, J. W., Fields, C, and Venter, J. C. (1992). Sequence identification of 2,375 human brain genes. Nature {London) 355, 632-634.
3. Ades, I. Z., and Butow, R. A. (1980). The products of mitochondria-bound cytoplasmic polysomes in yeast. J. Biol. Chem. 255, 9918-9924.
4. Agsteribbe, E., Huckriede, A., Veehuis, M., Ruiters, M. H. J., Niezen-Konig, K. E., Skjeldal, O. H., Skullerud, K., Gupta, R. S., Hallberg, R., van Diggelen, O. P., and Schölte, H. R. (1993). A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60. Biochem. Biophys. Res. Commun. 193(1), 146-154.
5. Alconada, A., Kübrich, M., Moczko, M., Hönlinger, A., and Pfanner, N. (1995). The mitochondrial receptor complex: The small subunit Mom8b/Isp6 supports association of receptors with the general insertion pore and transfer of preproteins. Mol. Cell Biol. 15, 6196-6205.
6. Amerik, A. Y., Petukhova, G. V., Grigorenko, V. G., Lykov, I. P., Yarovoi, S. V., Lipkin, V. M., and Gorbalenya, A. E. (1994). Cloning and sequence analysis of the cDNA for a human homolog of eubacterial ATP-dependent Lon proteases. FEES Lett. 340, 25-28.
7. Amin, J., Ananthan, J., and Voellmy, R. (1988). Key features of heat shock regulatory elements. Mol. Cell. Biol. 8, 3761-3769.
8. Ananthan, J., Goldberg, A. L., and Voellmy, R. (1986). Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 232, 522-524.
9. Anfinsen, C. B. (1973). Principles that govern the folding of proteins chains. Science 181, 223-230.
10. Ang, D., Chandrasekhar, G. N., Zylicz, M., and Georgopoulos, C. (1986). Escherichia coli grpE gene codes for heat shock protein B25.3, essential for both A DNA replication at all temperatures and host growth at high temperature. J. Bacterial. 167, 25-29.
11. Argan, C, Lusty, C. J., and Shore, G. C. (1983). Membrane and cytosolic components affecting transport of the precursor for ornithine carbamyltransferase into mitochondria. /. Biol. Chem. 258, 6667-6670.
12. Atencio, D. P., and Yaffe, M. P. (1992). MASS, a yeast homolog of DnaJ involved in mitochondria! protein import. Mol. Cell Biol. 12, 283-291.
13. Bach, J. F., and Antoine, B. (1968). In vitro detection of immunosuppressive activity of antilymphocyte sera. Nature (London) 217, 658-659.
14. Baker, K. P., Schaniel, A., Vestweber, D., and Schatz, G. (1990). A yeast mitochondria! outer membrane protein essential for protein import and cell viability. Nature (London) 348, 605-609.
15. Barker, R. N., Wells, A. D., Ghoraishian, M., Easterfield, A. J., Hitsumoto, Y., Elson, C. J., and Thompson, S. J. (1996). Expression of mammalian 60-kD heat shock protein in the joints of mice with pristane-induced arthritis. Clin. Exp. Immunol. 103, 83-88.
16. Beckmann, R. P., Mizzen, L. A., and Welch, W. J. (1990). Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248, 850-854.
17. Ben-Nun, A., Mendel, I., Sappier, G., and Kerlero de Rosbo, N. (1995). A 12-kDa protein of Mycobacterium tuberculosis protects mice against experimental autoimmune encephalomyelitis. /. Immunol. 154, 2939-2948.
18. +C, Klaus, C., Dietmeier, K., Neupert, W., and Brunner, M. (1995). The MIM complex mediates preprotein translocation across the mitochondria! inner membrane and couples it to the mt-Hsp70/ATP driving system. Cell 81,1085-1093.
19. Billingham, M. E., Carney, S., Butler, R., and Colston, M. J. (1990). A mycobacterial 65-kD heat shock protein induces antigen specific suppression of adjuvant arthritis, but is not itself arthritogenic. /. Exp. Med. 171, 339.
20. Birk, O. S., Douek, D. C., Elias, D., Takacs, K., Dewchmand, H., Gur, S. L., Walker, M. D., van der Zee, R., Cohen, I. R., and Altmann, D. (1996). A role of HspoO in autoimmune diabetes: Analysis in a transgenic model. Proc. Natl. Acad. Sei. USA 93, 1032-1037.
21. Birnbaum, G., Kotilinek, L., and Albrecht, L. (1993). Spinal fluid lymphocytes from a subgroup of multiple sclerosis patients respond to mycobacterial antigens. Ann. Neural. 34, 18-24.
22. Blom, J., Kiibrich, M., Rassow, J., Voos, W., Dekker, P. J. T., Maarse, A., Meijer, M., and Pfanner, N. (1993). The essential yeast protein MIM44 (encoded by MPI1) is involved in an early step of preprotein translocation across the mitochondrial inner membrane. Mol. Cell. Biol. 13, 7364-7371.
23. Blond-Elguindi, S., Cwiria, S. E., Dower, W. J., Lipshutz, R. J., Sprang, S. R., Sambrook, J. F., and Gething, M-J. H. (1993). Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728.
24. Bochkareva, E. S., and Girshovich, A. S. (1992). A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL. /. Biol. Chem. 267, 25672-25675.
25. Boisvert, D. C., Wang, J., Otwinowski, Z., Honvich, A. L., and Sigler, P. B. (1996). The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP-yS. Nature Struct. Biol. 3, 170-177.
26. Bolliger, L., Deloche, O., Glick, B. S., Georgopoulos, C, Jenö, P., Kronidou, N., Horst, M., Morishima, N., and Schatz, O. (1994). A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability. EMBO J. 13, 1998-2006.
27. Bolliger, L., Junne, T., Schatz, G., and Lithgow, T. (1995). Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria. EMBO J. 14, 6318-6326.
28. Borner, U., Pfanner, N., and Dietmeier, K. (1996). Identification of a third yeast mitochondrial Tom protein with tetratrico peptide repeats. FEBS Lett. 382, 153-158.
29. Bork, P., Sander, C, and Valencia, A. (1992). An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc. Natl. Acad. Sei. USA 89, 7290-7294.
30. Born, W., Hall, L., Dallas, A., Boymel, J., Shinnick, T., Young, D., Brennan, P., and O'Brien, R. (1990). Recognition of a peptide by heat shock reactive yS T lymphocytes. Science 249, 67-69.
31. Braig, K., Simon, M., Furuya, F., Hainfeld, J. F., and Horwich, A. L. (1993). A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proc. Natl. Acad. Sei. USA 90, 3978-3982.
32. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C, Joacimiak, A., Honvich, A. L., and Sigler, P. B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature (London) 371, 578-586.
33. Braig, K., Adams, P. D., and Brünger, A. T. (1995). Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Aresolution. Nature Struct. Biol. 2, 1083-1093.
34. Brosnan, C. F., Battistini, L., Gao, Y. L., Raine, C. S., and Aquino, D. A. (1996). Heat shock proteins and multiple sclerosis: A review. /. Neuropathol. Exp. Neural. 55, 389-402.
35. Bross, P., Andresen, B. S., Knudsen, I., Kruse, T. A., and Gregersen, N. (1995). Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene. FEBS Lett. 377, 249-252.
36. 1-ATPase β-subunit by CD and NMR spectroscopy. Biochim. Biophys. Acta 1159, 81-93.
37. Buchberger, A., Schröder, H., Büttner, M., Valencia, A., and Bukau, B. (1994). A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Struct. Biol. 1, 95-101.
38. Buchberger, A., Theyssen, H., Schröder, H., McCarty, J. S., Virgallita, G., Milkereit, P., Reinstein, J., and Bukau, B. (1995). Nucleotide-induced Conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. /. Biol. Cliem. 270, 16903-16910.
39. Burston, S. G., Ranson, N. A., and Clarke, A. R. (1995). The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249, 138-152.
40. Callebaut, I., and Mornon, J-P. (1995). Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family. FEBS Lett. 374, 211-215.
41. Caplan, A. J., and Douglas, M. G. (1991). Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein. /. Cell Biol. 114, 609-621.
42. Caplan, A. J., Tsai, J., Casey, P. J., and Douglas, M. G. (1992a). Farnesylation of YDJlp is required for function at elevated growth temperatures in Saccliaroinyces cerevisiae. J. Biol. Cliem. 267, 18890-18895.
43. Caplan, A. J., Cyr, D. M., and Douglas, M. G. (1992b). YDJ lp facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71,1143-1155.
44. Cavanagh, A., and Morton, H. (1994). The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10. Eur. J. Biochcm. 222,551-560.
45. Cavanagh, A. C., and Morton, H. (1996). EPF: Embryo detector and molecular chaperone. Today's Life Sei., May, 24-27.
46. Chappell, T. G., Konforti, B. B., Schmidt, S. L., and Rothman, J. E. (1987). The ATPase core of a clathrin uncoating protein. J. Biol. Chem. 262, 746-750.
47. Cheetham, M. E., Jackson, A. P., and Anderton, B. H. (1994). Regulation of 70-Da heatshock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJla and HSJlb. Eur. J. Biocliem. 226, 99-107.
48. Chen, S., Roseman, A. M, Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R., and Saibil, H. R. (1994). Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature (London) 371, 261-264.
49. Chen, W.-J., and Douglas, M. G. (1987). Phosphodiester bond cleavage outside mitochondria is required for the completion of protein import into the mitochondria! matrix. Cell 49, 651-658.
50. Cheng, M. Y., Hartl, F.-U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W., Hallberg, E. M., Hallberg, R. L., and Horwich, A. L. (1989). Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature (London) 337, 620-625.
51. Christopher, J. A., and Baldwin, T. O. (1996). Implications of N and C-terminal proximity for protein folding. J. Mol. Biol. 257, 175-187.
52. Clarke, A. R., and Lund, P. A. (1996). Kinetic and energetic aspects of chaperonin function. In "The Chaperonins" (R. J. Ellis, Ed.), pp. 167-212. Academic Press, San Diego.
53. Cohen, I. R., and Young, D. B. (1991). Autoimmunity, microbial immunity and the imunological homunculus. Immunol. Today 12, 105-110.
54. Corrales, F. J., and Fersht, A. R. (1996). Toward a mechanism for GroEL-GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage. Proc. Nail. Acad. Sci. USA 93, 4509-4512.
55. Craig, E. A., and Jacobsen, K. (1985). Mutations in cognate gene of Saccharomyces cerevisiae HSP70 result in reduced growth rates at low temperatures. AM. Cell. Biol. S, 3517-3524.
56. Craig, E. A., Kramer, J., and Kosic-Smithers, J. (1987). SSCI, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth. Proc. Natl. Acad. Set. USA 84, 4156-4160.
57. Craig, E. A., Kramer, J., Shilling, J., Werner-Washburne, M., Holmes, S., Kosic-Smithers, J., and Nicolet, C. M. (1989). SSCI, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein. Mol. Cell. Biol. 9, 3000-3008.
58. Crooke, E., and Wickner, W. (1987). Trigger factor: A soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc. Natl. Acad. Sei. USA 84, 5216-5220.
59. Cyr, D. M., Lu, X., and Douglas, M. G. (1992). Regulation of HSP70 function by a eukaryotic DnaJ homolog. /. Biol. Chem. 267, 20927-20931.
60. Cyr, D. M., Langer, T., and Douglas, M. G. (1994). DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70. Trends Biocliem. Sei. 19, 177-181.
61. Danieli, M. G., Candela, M., Ricciatti, A. M., Reginelli, R., Danieli, G., Cohen, I. R., and Gabrielli, A. (1992). Antibodies to mycobacterial 65kDa heat shock protein in systemic sclerosis (scleroderma). /. Autoimmunity 5, 443-452.
62. De Graeff-Meeder, E. R., van Eden, W., Rijkers, G. T., Prakken, B. J., Kuis, W., VoorhorstOgink, E. M., van der Zee, R., Schuurman, H. J., Helders, P. J. M., and Zegers, B. J. (1995). Juvenile chronic arthritis: T cell reactivity to human hsp60 in patients with a favorable course of arthritis. J. Clin. Invest. 95, 934-940.
63. Dekker, P. J. T., Keil, P., Rassow, J., Maarse, A. C, Pfanner, R, and Meijer, M. (1993). Identification of MIM23, a putative component of the protein import machinery of the mitochondrial inner membrane. FEBS Lett. 330, 66-70.
64. Desautels, M., and Goldberg, A. L. (1982). Demonstration of an ATP-dependent, Vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. J. Biol. Chem. 257, 11673-11679.
65. Deshaies, R. J., Koch, B. D., Werner-Washburne, M., Craig, E. A., and Schekman, R. (1988). A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature (London) 332, 800-805.
66. Edenhofer, F., Rieger, R., Famulok, M., Wendler, W., Weiss, S., and Winnaker, E. L. (1996). Prion protein PrPc interacts with molecular chaperones of the HSP60 family. /. Virol. 70, 4724-4728.
67. Eilers, M., and Schatz, G. (1986). Binding of a specific ligand inhibits import of a purified precursor into mitochondria. Nature (London) 322, 228-232.
68. Elias,'D., and Cohen, I. R. (1995). Treatment of autoimmune diabetes and insulitis in NOD mice with heat shock protein 60 peptide p277. Diabetes 44,1132-1138.
69. Elias, D., Reshef, T., Birk, O. S., van der Zee, R., Walker, M. D., and Cohen, I. R. (1990). Vaccination against autoimmune mouse diabetes with a T-cell epitope of the human 65-kDa heat shock protein. Proc. Natl. Acad. Sei. USA 88, 3088-3091.
70. Elias, D., Marcus, H., Reshef, T., Ablamunits, V., and Cohen, I. R. (1995). Induction of diabetes in standard mice by immunization with the p277 peptide of a 60-kDa heat shock protein. EUT. J. Immunol. 25, 2851-2857.
71. Ellis, J., and Hartl, F.-U. (1996). Protein folding in the cell: Competing models of chaperonin function. FASEB J. 10, 20-26.
72. Ellis, R. J. (1987). Proteins as molecular chaperones. Nature (London) 328, 378-379.
73. Ellis, R. J. (1996). Chaperonins: Introductory perspective. In "The Chaperonins" (R. J. Ellis, Ed.), pp. 2-25. Academic Press, San Diego.
74. Emmrich, F., Thole, J., van Embden, J., and Kaufmann, S. H. E. (1986). A recombinant 64 kDa protein of Mycobacterium bovis BCG specifically stimulates human T4 clones reactive to mycobacterial antigens. /. Exp. Med. 163, 1024-1029.
75. Emtage, J. L. T., and Jensen, R. E. (1993). MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway. /. Cell Biol. 122,1003-1012.
76. Endo, T., Shimada, I., Roise, D., and Inagaki, F. (1989). N-terminal half of a mitochondrial presequence takes a helical conformation when bound to dodecylphosphocholine micelles: A proton nuclear magnetic resonance study. J. Biochem. 106, 396-400.
77. Fayet, O., Ziegelhoffer, T., and Georgopoulos, C. (1989). The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. /. Bacterial. 171, 1379-1385.
78. Fenton, W. A., Kashi, Y., Furtak, K., and Horwich, A. L. (1994). Residues in chaperonin GroEL required for polypeptide binding and release. Nature (London) 371, 614-619.
79. Perm, M. T., Söderström, K., Jindal, S., Grönberg, A., Ivanyi, J., Young, R., and Kiessling, R. (1992). Induction of human hsp60 expression in monocytic cell lines. Int. Immunol. 4, 305-311.
80. Fernandes, M., O'Brien, T., and Lis, J. T. (1994). Structure and regulation of heat shock gene promoters. In "The Biology of Heat Shock Proteins and Molecular Chaperones" (R. I. Morimoto, A. Tissières, and C. Geogopoulos, Eds.), pp. 375-393 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
81. Ferrarini, M., Heltai, S., Zocchi, M. R., and Rugarli, C. (1992). Unusual expression and localization of heat-shock proteins in human tumour cells. Int. J. Cancer 51, 613-619.
82. Δ2 T cells of a GroEL homolog on Daudi Burkitt's lymphoma cells. Science 250, 1269-1273.
83. Fischer, H. P., Charrock, C. E. M., Colston, M. J., and Panayi, O.S. (1991). Limiting dilution analysis proliferative T cell responses to mycobacterial 65-kDa heat shock protein fails to show significant frequency differences between synovial fluid and peripheral blood of pa-tients with rheumatoid arthritis. Eur. J. Immunol. 21, 2937-2941.
84. Fitzgerald, M., and Keast, D. (1994). Fab fragments from the monoclonal antibody ML30 bind to treated human myeloid leukemia cells. FASEB J. 8, 259-261.
85. Flaherty, K. M., Deluca-FIaherty, C., and McKay, D. B. (1990). Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature (London) 346,623-628.
86. Flynn, G. C, Pohl, J., Flocco, M. T., and Rothman, J. E. (1991). Peptide-binding specificity of the molecular chaperone BiP. Nature (London) 353, 726-730.
87. Freedman, M. S., Buu, N. N., Ruijs, T. C. J., Williams, K., and Antel, J. P. (1992). Differential expression of heat shock proteins by human glial cells. /. Neuroimmunol. 41, 231-238.
88. Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F. U. (1994). Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature (London) 370,111-117.
89. Fu, Y-X., Cranfill, R., Vollmer, M., van der Zee, R., O'Brien, R. L., and Born, W. (1993). In vivo response of murine yA T cells to a heat shock protein-derived peptide. Proc. Natl. Acad. Sei. USA 90, 322-326.
90. +J., Schirra, C., Bujard, H., and Bukau, B. (1996). EMBO J. 15, 607-617.
91. Gao, Y. L., Brosnan, C. F., and Raine, C. S. (1995). Experimental autoimmune encephalomyelitis: Qualitative and semiquantitative differences in heat shock protein 60 expression in the central nervous system. J. Immunol. 154(7), 3548-3556.
92. Carrels, J. I. (1995). YPD-A database for the proteins of Saccharomyces cerevisiae. Nucleic Acid Res. 24, 46-49.
93. Gavel, Y., and von Heijne, G. (1990). Cleavage-site motifs in mitochondria! targeting peptides. Protein Eng. 4, 33-37.
94. Georgopoulos, C, Ang, D., Liberek, K., and Zylicz, M. (1990). Properties of the Escherichia coli heat shock proteins and their role in bacteriophage A growth. In "Stress Proteins in Biology and Medicine" (R. I. Morimoto, A. Tissières, and C. Georgopoulos, Eds.), pp. 191-221. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
95. Georgopoulos, C., Liberek, K., Zylicz., M., and Ang, D. (1994). Properties of heat shock proteins of Escherichia coli and the autoregulation of the heat shock response. In "The Biology of Heat Shock Proteins and Molecular Chaperones" (R. I. Morimoto, A. Tissières, and C. Georgopoulos, Eds.), pp. 209-249. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
96. Gething, M.-J., and Sambrook, J. (1992). Protein folding in the cell. Nature (London) 355, 33-45.
97. Gething, M-J., BIond-Elguindi, S., Mon, K., and Sambrook, J. F. (1994). Structure, function, and regulation of the endoplasmic reticulum chaperone, BiP. In "The Biology of Heat Shock Proteins and Molecular Chaperones" (R. I. Morimoto, A. Tissières, and C. Geogopoulos, Eds.), pp. 111-135. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
98. Click, B. (1995). Can HSP70 proteins act as force-generating motors? Cell 80, 11-14.
99. Glick, B., Wächter, C., and Schatz, G. (1991). Protein import into mitochondria: Two systems acting in tandem. Trends Cell Biol. 1, 99-103.
100. Glick, B., Beasley, E. M., and Schatz, G. (1992). Protein sorting in mitochondria. Trends Biochem. Sei. 17, 453-459.
101. Goff, S. A., Casson, L. P., and Goldberg, A. L. (1984). Heat shock regulatory gene htpR influences rates of protein degradation and expression of the Ion gene in Escherichia coli. Proc. Natl. Acad. Sei. USA 81, 6647-6651.
102. Goldberg, A. L. (1992). The mechanism and function of ATP-dependent proteases in bacterial and animal cells. Ear. J. Biochem. 203, 9-23.
103. Goping, I. S., Millar, D. G., and Shore, G. C. (1995). Identification of the human mitochondrial protein import receptor, huMas20p. Complementation of kmas20 in yeast. FEBS Lett. 373, 45-50.
104. Gottesman, S., and Maurizi, M. R. (1992). Regulation by proteolysis: Energy-dependent proteases and their targets. Microbiol. Rev. 56, 592-621.
105. Gottesman, S., Clark, W. P., De Crecy-Lagard, V., and Maurizi, M. R. (1993). ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 268, 22618-22626.
106. Gragerov, A., Zeng, L., Zhao, X., Burkholder, W., and Gottesman, M. E. (1994). Specificity of DnaK-peptide binding. /. Mol. Biol. 235, 848-854.
107. Gratzer, S., Lithgow, T., Bauer, R. E., Lamping, E., Paltauf, F., Kohhvein, S. D., Haucke, V., Jurihe, T., Schatz, G., and Horst, M. (1995). Mas37p, a novel receptor subunit for protein import into mitochondria. J. Cell Biol. 129, 25-34.
108. Gray, M. W. (1989). The evolutionary origins of organelles. Trends Genet. 5, 294-299.
109. Grossman, A. D., Erickson, J. W., and Gross, C. A. (1984). The htpR gene product of E. coli is a sigma factor for Heat-shock proteins. Cell 38, 383-390.
110. Hachiya, N., Alam, R., Sakasegawa, Y., Sakaguchi, M., Mihara, K., and Omura, T. (1993). A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins. EMBO J. 12, 1579-1586.
111. Hachiya, N., Komiya, T., Alam, R., Iwahashi, J., Sakaguchi, M., Omura, T., and Mihara, K. (1994). MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria. EMBO J. 13, 5146-5154.
112. Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G., and Lithgow, T. (1995). Reconstitution of the initial steps of mitochondrial protein import. Nature (London) 376, 705-709.
113. +energy states. Biochemistry 61, 598-605.
114. Hallberg, E. M., Shu, Y., and Hallberg, R. L. (1993). Loss of mitochondrial hsp60 function: Nonequivalent effects on matrix-targeted and intermembrane-targeted proteins. Mol. Cell. Biol. 13, 3050-3057.
115. Hammen, P. K., Gorenstein, D. G., and Weiner, H. (1994). Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import. Biochemistry 33, 8610-8617.
116. Hansen, W. J., Lingappa, V. R., and Welch, W. J. (1994). Complex environment of nascent polypeptide chains. /. Biol. Chem. 269, 26610-26613.
117. Hanson, B., Nuttall, S., and Hoogenraad, N. (1996). A receptor for the import of proteins into human mitochondria. Ettr. J. Biocliem. 235, 750-753.
118. Hare, J. F. (1990). Mechanisms of membrane protein turnover. Biocliem. Biophys. Acta 1031, 71-90.
119. Hartl, F.-U. (1994). Secrets of a double-doughnut. Nature (London) 371, 557-559.
120. Hartl, F.-U. (1996). Molecular chaperones in cellular protein folding. Nature (London) 381, 571-580.
121. Hartl, F-U., Pfanner, N., Nicholson, D. W., and Neupert, W. (1989). Mitochondrial protein import. Biochim. Biophys. Acta 988, 1-45.
122. Hartman, D. J., Hoogenraad, N. J., Condron, R., and Hoj, P. B. (1992). Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro. Proc. Nail. Acad. Sei. USA 89, 3394-3398.
123. Hartman, D. J., Surin, B. P., Dixon, N. E., Hoogenraad, N. J., and Høj, P. B. (1993). Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro. Proc. Natl. Acad. Sei. USA 90, 2276-2280.
124. Hattori, H., Liu, Y.-C, Tohnai, I., Ueda, M., Kaneda, T., Kobayashi, T., Tanabe, K., and Ohtsuka, K. (1992). Intracellular localization and partial amino acid sequence of a stressinducible 40-kDa protein in HeLa cells. Cell Struct. Fund. 17, 77-86.
125. Haucke, V., Lithgow, T., Rospert, S., Hahne, K., and Schatz, G. (1995). The yeast mitochondrial protein import receptor Mas20p binds precursor proteins through electrostatic interaction with the positively charged presequence. /. Biol Client. 270, 5565-5570.
126. Haucke, V., Horst, M., Schatz, G., and Lithgow, T. (1996). The Mas20p and Mas70p subunits of the protein import receptor of yeast mitochondria interact via the tetratricopeptide repeat motif in Mas20p: Evidence for a single hetero-oligomeric receptor. EMBOJ. 15,1231-1237.
127. Hayer-Hartl, M. K., Martin, J., and Hartl, F. U. (1995). Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science 269, 836-841.
128. Hayes, S. A., arid Dice, J. F. (1996). Roles of molecular chaperones in protein degradation. J. Cell Biol. 132, 255-258.
129. Hemmingsen, S. M., Woolford, C., van der Vies, S. M., Tilly, K., Dennis, D. T., Georgopoulos, C. P., Hendrix, R. W., and Ellis, R. J. (1988). Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature (London) 333, 330-334.
130. Hendrick, J. P., Langer, T., Davis, T. A., Hartl, F. U., and Wiedmann, M. (1993). Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Nail. Acad. Sei. USA 90,10216-10220.
131. Hentschel, C. C, and Birnstiel, M. L. (1981). The organisation and expression of histone gene families. Cell 25, 301-313.
132. 32, the heat shock regulator in Esclierichia coli, is governed by HflB. Proc. Natl. Acad. Sei. USA 92,3516-3520.
133. Heufelder, A. E., Wenzel, B. E., and Bahn, R. S. (1992). Cell surface localization of a 72 kilodalton heat shock protein in retroocular fibroblasts from patients with Graves' opthalmopathy. J. Clin. Endocrinol. Metab. 74, 732-736.
134. Hindersson, P., Høiby, N., and Bangsborg, J. (1991). Sequence analysis of the Legionella micdadei groELS operon. FEMS Microbiol. Lett. 77, 31-38.
135. Hogervorst, E. J. M., Wagenaar, J. P. A., Boog, C. J. P., van der Zee, R., van Embden, J. D. A., and van Eden, W. (1992). Adjuvant arthritis and immunity to the mycobacterial 65 kDa heat shock protein. Int. Immunol. 4, 719-724.
136. Höhfeld, J., and Hartl, F. U. (1994). Role of chaperonin cofactor hsplO in protein folding and sorting in yeast mitochondria. J. Cell Biol. 126, 305-315.
137. Höhfeld, J., Minami, Y., and Hartl, F. U. (1995). Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle. Cell S3, 589-598.
138. Holoshitz, J., Koning, F., Coligan, J. E., DeBruyn, J., and Strober, S. (1989). Isolation of CD4" CDS'mycobacterium-reactive T lymphocyte clones from rheumatoid arthritis synovial fluid. Nature (London) 339, 226-229.
139. Hönlinger, A., Kübrich, M., Moczko, M., Gärtner, F., Mallet, L., Bussereau, F., Eckerskorn, C, Lottspeich, F., Dietmeier, K., Jacquet, M., and Pfanner, N. (1995). The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins. Mol. Cell Biol. 15, 3382-3389.
140. Hönlinger, A., Bömer, U., Alconada, A., Eckerskorn, C., Lottspeich, F., Dietmeier, K., and Pfanner, N. (1996). Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein import. EMBO J. IS, 2125-2137.
141. Horst, M., Hilfiker-Rothenfluh, S., Oppliger, W., and Schatz, G. (1995). Dynamic interaction of the protein translocation systems in the inner and outer membranes of yeast mitochondria. EMBO J. 14, 2293-2297.
142. Horwich, A. L., Brooks Low, K., Fenton, W. A., Hirshfield, I. N., and Furtak, K. (1993). Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL. Cell 74, 909-917.
143. Hunt, J. F., Weaver, A. J., Landry, S. J., Gierasch, L., and Deisenhofer, J. (1996). The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Nature (London) 379, 37-45.
144. Hutchinson, E. G., Tichelaar, W., Hofhaus, G., Weiss, H., and Leonard, K. R. (1989). Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochondria. EMBO J. 8, 1485-1490.
145. Ikeda, E., Yoshida, S., Mitsuzawa, H., Uno, L, and Toh-e, A. (1994). YGE1 is a yeast homologue of Eschericia coli grpE and is required for maintenance of mitochondrial functions. FEBS Lett. 339, 265-268.
146. Jaenicke, R. (1995). Folding and association versus misfolding and aggregation of proteins. Philos. Trans. R. Soc. London. B 348, 97-105.
147. Jarvis, J. A., Ryan, M. T., Hoogenraad, N. J., Craik, D. J., and Høj, P. B. (1995). Solution structure of the acetylated and noncleavable targeting signal of rat Chaperonin 10. /. Biol. Chem. 270, 1323-1331.
148. Jenséh, R. E., and Yaffe, M. P. (1988). Import of proteins into yeast mitochondria: The nuclear MAS2 gene encodes a component of the processing protease that is homologous to the AMS/-encoded subunit. EMBO J. 7, 3863-3871.
149. Jindal, S., Dudani, A. K., Singh, B., Harley, C. B., and Gupta, R. S. (1989). Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. Mol. Cell. Biol. 9, 2279-2283.
150. Jones, D. B., Coulson, F. W., and Duff, G. W. (1993). Sequence homologies between hsp60 and autoantigens. Immunol. Today 14,115-118.
151. Kalousek, F., Neupert, W., Omura, T., Schatz, G., and Schmilz, U. K. (1993). Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins. Trends Biochem. Sei. 18, 249.
152. Kandror, O., Busconi, L., Sherman, M., and Goldberg, A. L. (1994). Rapid degradation of an abnormal protein in Eschericia coli involves the chaperones GroEL and GroES. /. Biol. Chem. 269, 23575-23582.
153. Kandror, O., Sherman, M., Rhode, M., and Goldberg, A. L. (1995). Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J. 14, 6021-6027.
154. Kang, P.-J., Ostermann, J., Shilling, J., Neupert, W., Craig, E. A., and Pfanner, N. (1990). Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature (London) 348, 137-143.
155. Karslake, C, Piotto, M. E., Pak, Y. K., Weiner, H., and Gorenstein, D. G. (1990). 2D NMR and structural model for a mitochondrial signal peptide bound to a micelle. Biochemistry 29, 9872-9878.
156. Kaufmann, S. H. E. (1990). Heat shock proteins and the immune response. Immunol Today 11,129-136.
157. Kaufmann, S. H. E. (1994). Heat shock proteins and autoimmunity: A critical appraisal. Int. Arch. Allergy Immunol. 103, 317-322.
158. Kaufmann, S. H. E., and Schoel, B. (1994). Heat shock proteins as antigens in immunity against infection and self. The biology of heat shock proteins. Curr. Topics Microbiol. Immunol. 167, 191-205.
159. Kaur, I., Voss, S. D., Gupta, R. S., Schell, K., Fisch, P., and Sondel, P. M. (1993). Human peripheral yA T cells recognize hspoO molecules on Daudi Burkitt's lymphoma cells. J. Immunol. 150, 2046-2055.
160. Kellems, R. E., and Butow, R. A. (1972). Cytoplasmic-type 80 S ribosomes associated with yeast mitochondria. /. Biol Chem. 247, 8043-8050.
161. Kessel, M., Maurizi, M. R., Kim, B., Kocsis, E., Trus, B. L., Singh, S. K., and Steven, A. C. (1995). Homology in the structural organisation between E. coli ClpAP protease and the Eukaryotic 26 S proteasome. /. Mol. Biol. 250, 587-594.
162. Kiebler, M., Pfaller, R., Söllner, T., Griffiths, G., Horstman, H., Pfanner, N., and Neupert, W. (1990). Identification of a mitochondrial receptor complex required for recognition and membrane insertion of precursor proteins. Nature (London) 348, 610-616.
163. Kiebler, M., Keil, P., Schneider, H., van der Klei, I. J., Pfanner, N., and Neupert, W. (1993). The mitochondrial receptor complex: A central role of MOM22 in mediating preprotein transfer from receptors to the general insertion pore. Cell 74, 483-492.
164. Komiya, T., Sakaguchi, M., and Mihara, K. (1996). Cytoplasmic chaperones determine the targeting pathway of precursor proteins to mitochondria. EMBO J. 15, 399-407.
165. Kozak, M. (1989). The scanning model for translation, an update. /. Cell Biol. 108, 229-241.
166. Kronidou, N. G., Oppliger, W., Bolliger, L., Hannavy, K., Click, B. S., Schatz, G., and Horst, M. (1994). Dynamic interaction between Isp45 and mitochondria! hsp70 in the protein import system of the yeast mitochondrial inner membrane. Proc. Natl Acad. Sei. USA 91, 12818-12822.
167. Kübrich, M., Keil, P., Rassow, J., Dekker, P. J. T., Blom, J., Meijer, M., and Pfanner, N. (1994). The pölytopic mitochondrial inner membrane proteins MIM17 and MIM23 operate at the same preprotein import site. FEBS Lett. 349, 222-228.
168. Kübrich, M., Dietmeier, K., and Pfanner, N. (1995). Genetic and biochemical dissection of the mitochondrial protein-import machinery. Ctirr. Genet. 27, 393-403.
169. Kunau, W. H., Beyer, A., Franken, T., Gölte, K., Marzioch, M., Saidowsky, J., SkaletzRorowski, A., and Wiebel, F. F. (1993). Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae. Biochimie 75, 209-224.
170. Kutejovd, E., Durcová, G., Surovková, E., and Kuzela, Š. (1993). Yeast mitochondrial ATP-dependent protease: Purification and comparison with the homologous rat enzyme and the bacterial ATP-dependent protease La. FEBS Lett. 329, 47-50.
171. Lai, N-S., Lan, J-L., Yu, C-L., and Lin, R-H. (1995). Antibody to Mycobacterium tuberculosis 65kDa heat shock protein in patients with rheumatoid arthritis-A survey of antigen-specific antibody isotypes and subclasses in an endemic area of previous tuberculosis infection. Ann-Rheum. Dis. 54, 225-228.
172. Landry, S. J., and Gierasch, L. M. (1991). The chaperonin GroEL binds a polypeptide in and a-helical conformation. Biochemistry 30, 7359-7362.
173. Landry, S. J., Jordan, R., McMacken, R., and Gierasch, L. M. (1992). Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature (London) 355, 455-457.
174. Landry, S. J., Zeilstra-Ryalls, J., Fayet, O., Georgopoulos, C., and Gierasch, L. M. (1993). Characterization of a functionally important domain of GroES. Nature (London) 364, 255-258.
175. Langer, T., Pfeifer, G., Martin, J., Baumeister, W., and Hartl, F.-U. (1992a). Chaperoninmediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757-4765.
176. Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K., and Hartl, F.-U. (1992b). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature (London) 356, 683-689.
177. Laskey, R. A., Honda, B. M., Mills, A. D., and Finch, J. T. (1978). Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature (London) 275, 416-420.
178. Layloraya, S., Gambill, B. D., and Craig, E. A. (1994). A role for a eukaryotic GrpE-related protein, Mgelp, in protein translocation. Proc. Natl. Acad. Sei. USA 91, 6481-6485.
179. Layloraya, S., Dekker, P. J. T., Voos, W., Craig, E. A., and Pfanner, N. (1995). Mitochondrial GrpE modulates the function of matrix hsp70 in translocation and maturation of preproteins. Mol. Cell. Biol. 15, 7098-7105.
180. Lee, F.-J. S., Lin, L.-W., and Smith, J. A. (1989). N" acetylation is required for normal growth and mating of Saccharomyces cerevisiae. J. Bacterial. 171, 5795-5802.
181. Legname, G., Fossati, G., Gromo, G., Monzini, N., Marcucci, F., and Modena, D. (1995). Expression in Eschericia coli, purification and functional activity of recombinant human chaperonin 10. FEBS Lett. 361, 211-214.
182. Leonhardt, S. A., Fearon, K., Danese, P. N., and Manson, T. L. (1993). HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent protease. Mol. Cell. Biol. 13, 6304-6313.
183. Lesser, G. J., and Rose, G. D. (1990). Hydrophobicity of amino acid subgroups in proteins. Proteins Struct. Fund. Genet. 8, 6-13.
184. Leustek, T., Dalie, B., Amir-Shapira, D., Brot, N., and Weissbach, H. (1989). A member of the hsp70 family is localized in mitochondria and resembles Eschericliia coli DnaK. Proc. Nail. Acad. Sei. USA 86, 7805-7808.
185. Liberek, K., Marszalek, J., Ang, D., and Georgopoulos, C. (1991a). Eschericliia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sei. USA 88, 2874-2878.
186. Liberek, K., Skowyra, D., Zylicz, M., Johnson, C, and Georgopoulos, C. (1991b). The Eschericliia coli DnaK chaperone protein, the Hsp70 eukaryotic equivalent, changes its conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. /. Biol. Cliem. 266, 14491-14496.
187. Life, P., Hassell, A., Williams, K., Young, S., Bacon, P., Southwood, T., and Gaston, J. S. (1993). Responses to Gram negative enteric bacterial antigens by synovial T cells from patients with juvenile chronic arthritis: Recognition of heat shock protein HSP60. /. Rheuma-tot. 20, 1388-1396.
188. Lill, R., Stuart, R. A., Drygas, M. E., Nargang, F. E., and Neupert, W. (1992). Import of cytochrome c heme lyase into mitochondria: A novel pathway into the intermembrane space. EMBO J. 11, 449-456.
189. Lindquist, S., Patino, M. M., Chernoff, Y. O., Kowal, A. S., Singer, M. A., Liebman, S. W., Lee, K. H., and Blake, T. (1995). The role of HSP104 in stress tolerance and [PSI+] propagation in Saccharomyces cerevisiae Cold Spring Harbor Synip Quant. Biol. 60,451-460.
190. Linton, J. P., Yen, J.-Y. J, Selby, E., Chen, Z., Chinsky, J. M., Liu, K., Kellens, R. E., and Grouse, G. F. (1989). Dual bidirectional promoters at the mouse dhfr locus: Cloning and characterisation of two mRNA classes of the divergently transcribed REP-1 gene. Mol. Cell. Biol. 9, 3058-3072
191. Lithgow.T., Hoj, P. B., and Hoogenraad, N. J. (1993a). Do cytosolic factors prevent promiscuity at the membrane surface? FEES Lett. 329, 1-4.
192. Lithgow, T., Ryan, M., Anderson, R., Hoj, P. B., and Hoogenraad, N. J. (1993b). A constitutive form of heat-shock protein 70 is located in the outer membranes of mitochondria from rat liver. FEES Lett. 332, 277-281.
193. Lithgow, T., Junne, T., Suda, K., Gratzer, S., and Schatz, G. (1994). The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast. Proc. Natl Acad. Sei USA 91, 11973-11977.
194. Lithgow, T., Click, S., and Schatz, G. (1995). The protein import receptor of mitochondria. Trends Biochem. Sei. 20, 98-101.
195. Lorimer, G. H. (1996). A quantitative assessment of the role of the chaperonin proteins in protein folding in vitro. FASEB J. 10, 5-9.
196. Lubben, T. H., Gatenby, A. A., Donaldson, G. K., Lorimer, G. H., and Viitanen, P. V. (1990). Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. Proc. Natl. Acad. Sei. USA 87, 7683-7687.
197. Luke, M. M., Sutton, A., and Arndt, K. T. (1991). Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. /. Cell Biol. 114, 623-638.
198. Maarse, A. C, Blom, J., Grivell, L. A., and Meijer, M. (1992). MPI1, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria. EMBO J. 11, 3619-3628.
199. Maarse, A. C, Blom, J., Keil, P., Pfanner, N., and Meijer, M. (1994). Identification of the essential yeast protein MIM17, an integral mitochondrial inner membrane protein involved in protein import. FEES Lett. 349, 215-221.
200. MacLachlan, L. K., Harris, P. I., Reid, D. G., White, J., Chapman, D., Lucy, J. A., and Austen, B. M. (1994). A spectroscopic study of the mitochondrial transit peptide of rat malate dehydrogenase. Biochem J. 303, 657-662.
201. Mande, S. C, Mehra, V., Bloom, B. R., and Hol, W. G. J. (1996). Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. Science 271, 203-207.
202. Manning-Krieg, U. C., Scherer, P. E., and Schatz, G. (1991). Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10, 3273-3280.
203. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and Hartl, F.-U. (1991). Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'like intermediate. Nature (London) 352, 36-42.
204. Martin, J., Horwich, A. L., and Hartl, F.-U. (1992). Prevention of protein denaturation under heat stress by the chaperonin hsp60. Science 258, 995-998.
205. Martinus, R. D., Garth, G. P., Webster, T. L., Cartwright, P., Naylor, D. J., Høj, P. B., and Hoogenraad, N. J. (1996). Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome. Eur. J. Biochem. 240, 98-103.
206. Masison, D. C, and Wickner, R. B. (1995). Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270, 93-95.
207. Matouschek, A., Rospert, S., Schmid, K., Click, B. S., and Schatz, G. (1995). Cyclophilin catalyzes protein folding in yeast mitochondria. Proc. Natl. Acad. Sei. USA 92, 6319-6323.
208. Maurizi, M. R., Clark, W. P., Kim, S-H., and Gottesman, S. Clp P represents a unique family of serine proteases. /. Biol. Chein. 265, 12546-12552.
209. Mayer, A., Lill, R., and Neupert, W. (1993). Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria. /. Cell Biol. 121, 1233-1243.
210. Mayer, A., Nargang, F. E., Neupert, W., and Lill, R. (1995). MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19. EMBO J. 14,4204-4211.
211. Mayhew, M., da Suva, A. C. R., Martin, J., Erdjument-Bromage, H., Tempst, P., and Hartl, F. U. (1996). Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature (London) 379, 420-426.
212. McMullin, T. W., and Hallberg, R. L. (1987). A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetraliymena tliermophila, Mol. Cell. Biol. 7, 4414-4423.
213. McMullin, T. W., and Hallberg, R. L. (1988). A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene. Mol. Cell. Biol. 8, 371-380.
214. Mihara, K., and Omura, T. (1996). Cytoplasmic chaperones in precursor targeting to mitochondria: The role of MSF and hsp70. Trends Cell Biol. 6, 104-108.
215. Mitra, P. K., Mehra, N. K., Maiti, T. K., Banerjee, A., Taneja, V., Rajalingam, R., Ahuja, R. K., and Bhattacharya, B. C. (1995). Cd4+ T-cell responses to recombinant hsp65 and hsplS of M. leprae and their trypsin digested fragments in leprosy-Diversity in HLA-DR restriction. Int. J. Leprosy 63(4), 518-528.
216. Miura, S., Mori, M., and Tatibana, M. (1983). Transport of ornithine carbamoyltransferase precursor into mitochondria: Stimulation by potassium ion, magnesium ion and a reticulocyte cytosolic protein(s). J. Biol. Cliem. 258, 6671-6674.
217. Mizzen, L. A., Chang, C, Garrels, J. I., and Welch, W. J. (1989). Identification, characterization and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. /. Biol. Client. 264, 20664-20675.
218. Moczko, M., Dietmeier, K., Söllner, T., Segui, B., Steger, H. F., Neupert, W., and Pfanner, N. (1992). Identification of the mitochondrial receptor complex in Saccltaromyces cerevisiae. FEBS Lett. 310, 265-268.
219. Moczko, M., Ehmann, B., Gärtner, F., Hönlinger, A., Schäfer, E., and Pfanner, N. (1994). Deletion of the receptor MOM19 strongly impairs import of cleavable preproteins into Saccharoinyces cerevisiae mitochondria. J. Biol. Cliem. 269, 9045-9051.
220. Moczko, M., Schönfisch, B., Voos, W., Pfanner, N., and Rassow, J. (1995). The mitochondrial CIpB homolog Hsp78 cooperates with matrix Hsp70 in the maintenance of mitochondrial function. J. Mol. Biol. 254, 538-543.
221. Multhoff, G., Botzier, C, Wiesnet, M., Muller, E., Meier, T., Wilmanns, W., and Issels, R. D. (1995). A stress-inducible 72kDa heat shock protein (Hsp72) is expressed on the surface of human tumor cells, but not on normal cells. Int. J. Cancer 61, 272-279.
222. Murakami, K., and Mori, M. (1990). Purified presequence binding factor (PBF) forms an import-competent complex with a purified mitochondrial precursor protein. EMBO J. 9, 3201-3208.
223. Murakami, H., Pain, D., and Blobel, G. (1988a). 70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria. J. Cell Biol.-107, 2051-2057.
224. Murakami, K., Amaya, Y., Takiguchi, M., Ebina, Y., and Mori, M. (1988b). Reconstitution of mitochondrial protein transport with purified ornithine carbamoyltransferase precursor expressed in Escherichia coli. J. Biol. Chem. 263,18437-18442.
225. Murakami, K., Tokunaga, F., Iwanaga, S., and Mon, M. (1990). Presequence does not prevent folding of a purified mitochondrial precursor protein and is essential for association with a reticulocyte cytosolic factor(s). /. Biochem. 108, 207-214.
226. Murakami, K., Tanase, S., Morino, Y., and Mori, M. (1992). Presequence binding factordependent and -independent import of proteins into mitochondria. J. Biol. Chem. 267, 13119-13122.
227. Nakai, M., Endo, T., Hase, T., and Matsubara, H. (1993). Intramitochondrial protein sorting. J. Biol. Chem. 268, 24262-24269.
228. Naylor, D. J., Ryan, M. T., Condron, R., Hoogenraad, N. J., and Høj, P. B. (1995). Affinity purification and identification of GrpE homologues from mammalian mitochondria. Biochim. Biophys. Acta 1248, 75-79.
229. Naylor, D. J., Hoogenraad, N. J., and Høj, P. B. (1996). Isolation and characterisation of a cDNA encoding rat mitochondrial GrpE, a stress inducible chaperone of ubiquitous appearance in mammalian organs. FEBS Lett. 396, 181-188.
230. Nelson, R. J., Ziegelhoffer, T., Nicolet, C., Werner-Washburne, M., and Craig, E. A. (1992). The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71, 97-105.
231. Neupert, W., Hartl, F-U., Craig, E. A., and Pfanner, N. (1990). How do polypeptides cross the mitochondrial membranes? Cell 63, 447-450.
232. Nobrega, F. G., Nobrega, M. P., and Tzagoloff, A. (1992). BCS1, a novel gene required for the expression of functional Rieske iron-sulphur protein in Saccharomyces cerevisiae. EMBO J. 11, 3821-3829.
233. Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.-J., and Sambrook, J. (1989). S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57, 1223-1236.
234. O'Brien, R. L., Happ, M. P., Dallas, A., Cranfill, R., Hall, L., Lang, J., Fu, Y-X., Kubo, R., and Born, W. (1991). Recognition of a single Hsp60 epitope by an entire subset of γδ T lymphocytes. Immunol. Rev. 121,155-170.
235. O'Brien, R. L., Fu, Y-X., Cranfill, R., Dallas, A., Ellis, C, Reardon, C, Lang, J., Carding, S. R., Kubro, R., and Born, W. (1992). Heat shock protein hsp60-reactive yd cells: A large, diversified T-lymphocyte subset with highly focused specificity. Proc. Natl. Acad. Sei. USA 89, 4348-4352.
236. Ohba, M., and Schatz, G. (1987). Disruption of the outer membrane restores protein import to trypsin-treated yeast mitochondria. EMBO J. 6, 2109-2115.
237. Ohta, S., and Schatz, G. (1984). A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria. EMBO J. 3, 651-657.
238. Okazaki, A., Ikura, T., Nikaido, K., and Kuwajima, K. (1994). The chaperonin GroEL does not recognise apo-a-lactalbumin in the molten globule state. Struct. Biol. 1, 439-445.
239. Ostermann, J., Horwich, A. L., Neupert, W., and Hartl, F.-U. (1989). Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature (London) 341, 125-130.
240. Ostermann, J., Voos, W., Kang, P. J., Craig, E. A., Neupert, W., and Pfanner, N. (1990). Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix. FEES Lett. 277, 281-284.
241. Pajic, A., Tauer, R., Feldmann, H., Neupert, W., and Langer, T. (1994). YtalOp is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. FEBS Lett. 353, 201-206.
242. Palleros, D. R., Welch, W. J., and Fink, A. L. (1991). Interaction of hsp70 with unfolded proteins: Effects of temperature and nucleotides on the kinetics of binding. Proc. Natl. Acad. Sei. USA'SS, 5719-5723.
243. Parsell, D. A., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496.
244. Parsell, D. A., Kowal, A. S., Singer, M. A., and Linquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hspl04. Nature (London) 372, 475-478.
245. Patino, M. M., Liu, J-J., Glover, J. R., and Lindquist, S. (1996). Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273, 622-626.
246. Pchelintseva, O., Pak, Y. K., and Weiner, H. (1995). Identification of protein-receptor components required for the import of prealdehyde dehydrogenase into rat liver mitochondria. Arch. Biochem. Biophys. 323, 54-62.
247. Pelham, H. R. B. (1986). Speculations on the functions of the major heat shock and glucoseregulated proteins. Cell 46, 959-961.
248. Peralta, D., Hartman, D. J., Mclntosh, A. M., Hoogenraad, N. J., and Høj, P. B. (1990). cDNA and deduced amino acid sequence of rat liver prehspoO (chaperonin-60). Nucleic Acids Res. 18, 7162.
249. Peralta, D., Lithgow, T., Hoogenraad, N. J., and Hoj, P. B. (1993). Prechaperonin 60 and preornithine transcarbamylase share components of the import apparatus but have distinct maturation pathways in rat liver mitochondria. Ear. J. Biochem. 211, 881-889.
250. Peralta, D., Hartman, D. J., Hoogenraad, N. J., and Hpj, P. B. (1994). Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. FEBS Lett. 339, 45-49.
251. Perisic, O., Xiao, H., and Lis, J. T. (1989). Stable binding of Drosophila heat shock factor to head-head and tail-tail repeats of a conserved 5 bp recognition unit. Cell 59, 797-806.
252. Ferryman, R. A., Mooney, B., and Harmey, M. A. (1995). Identification of a 42-kDa plant mitochondrial outer membrane protein, MOM42, involved in the import of precursor proteins into plant mitochondria. Arch. Biochem. Biophys 316, 659-664.
253. Pfanner, N., and Meijer, M. (1995). Pulling in the proteins. Curr. Biol. 5, 132-135.
254. Pfanner, N., Hartl, F.-U., and Neupert, W. (1988). Import of proteins into mitochondria: A multi-step process. Enr. J. Biochem. 175, 205-212.
255. Pfanner, N., Rassow, J., Wienhues, U., Hergesberg, C, Sollner, T., Becker, K., and Neupert, W. (1990). Contact sites between inner and outer membranes: Structure and role in protein translocation into the mitochondria. Biochim. Biophys. Acta 1018, 239-242.
256. Pfanner, N., Rassow, J., van der Klei, I. J., and Neupert, W. (1992). A dynamic model of the mitochondrial protein import machinery. Cell 68, 999-1002.
257. Pfanner, N., Craig, E., and Meijer, M. (1994). The protein import machinery of the mitochondrial inner membrane. Trends Biochem. Sei. 19, 368-372.
258. Pfanner, N., Douglas, M. G., Endo, T., Hoogenraad, N. J., Jensen, R. E., Meijer, M., Neupert, W., Schatz, G., Schmilz, U. K., and Shore, G. C. (1996). Uniform nomenclature for the protein transport machinery of the mitochondrial membranes. Trends Biochem. Sei. 21, 51-52.
259. Picketts, D. J., Mayanil, C. S. K., and Gupta, R. S. (1989). Molecular cloning of a Chinese hamster mitochondrial protein related to the "chaperonin" family of bacterial and plant proteins. /. Biol. Chem. 264,12001-12008.
260. Pochon, N. A., and Mach, B. (1996). Genetic complexity of the human hsp 60 gene. Int. Immun. 8, 221-230.
261. Prabhakar, S., Kurien, E., Gupta, R. S., Zielinski, S., and Freedman, M. S. (1994). Heat shock protein immunoreactivity in CSF: Correlation with oligoclonal banding and demyelinating disease. Neurology 44, 1644-1648.
262. Prusiner, S. B. (1994). Biology and genetics of prion diseases. Anna. Rev. Microbiol. 48, 655-686.
263. Ptitsyn, O. B. (19S1). Protein folding: General physical model. FEES Lett. 131, 197-202.
264. Ragno, S., Winrow, V. R., Mascagni, P., Lucietto, P., DiPierro, F., Morris, C. J., and Blake, D. P. (1996). A synthetic 10-kD heat shock protein (hsplO) from Mycobacterimn tuberculosis modulates adjuvant arthritis. Clin. Exp. Immunol. 103, 384-390.
265. Randall, S. K., and Shore, G. C. (1989). Import of a mutant mitochondrial precursor fails to respond to stimulation by a cytosolic factor. FEBS Lett. 250, 561-564.
266. Rassow, J., Maarse, A. C, Krainer, E., Kübrich, M., Müller, H., Meijer, M., Craig, E. A., and Pfanner, N. (1994). Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Dial. 127,1547-1556.
267. Rassow, J., Mohrs, K., Koidl, S., Barthelmess, I. B., Pfanner, N., and Tropschug, M. (1995). Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell Biol. 15, 2654-2662.
268. Rebbe, N. F., Hickman, W. S., Ley, T. J., Stafford, D. W., and Hickman, S. (1989). Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene. J. Biol. Cliem. 264, 15006-15011.
269. Reid, G. A., and Schatz, G. (1982). Import of proteins into mitochondria: Yeast cells grown in the presence of carbonyl cyanide m-chlorophenylhydrazone accumulate massive amounts of some mitochondrial precursor polypeptides. J. Biol. Chein. 257, 13056-13061.
270. Res, P. C. M, Schaar, C. G., Breedveld, F. C., van Eden, W., van Embden, J. D. A., Cohen, I. R., and de Vries, R. R. P. (1988). Synovial fluid T cell reactivity against 65kDa heat shock protein of Mycobacteria in early chronic arthritis. Lancet, 478-480.
271. Richarme, G., and Kohiyama, M. (1994). Amino acid specificity of the Eschericia coli chaperone GroEL (heat shock protein 60). J. Biol. Cliem. 269, 7095-7098.
272. Ritossa, F. (1962). A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 18, 571-573.
273. Rospert, S., Click, B. S., Jenö, P., Schatz, G., Todd, M. J., Lorimer, G. H., and Viitanen, P. V. (1993a). Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Proc. Natl. Acad. Sei. USA 90, 10967-10971.
274. Rospert, S., Junne, T., Click, B. S., and Schatz, G. (1993b). Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES. FEBS Lett. 335, 358-360.
275. Rospert, S., Looser R., Dubaquie, Y., Matouschek, A., Click, B. S., and Schatz, G. (1996). Hsp60-independent protein folding in the matrix of yeast mitochondria. EMBO J. 15, 764-774.
276. Rowley, N., Prip-Buus, C., Westermann, B., Brown, C., Schwarz, E., Barrel, B., and Neupert, W. (1994). Mdjlp, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77, 249-259.
277. Ryan, M. T., Hoogenraad, N. J., and Hoj, P. B. (1994). Isolation of a cDNA clone specifying rat chaperonin 10, a stress inducible mitochondrial matrix protein synthesised without a cleavable presequence. FEBS Lett. 337, 152-156.
278. Ryan, M. T., Naylor, D. J., Hoogenraad, N. J., and Hoj, P. B. (1995). Affinity purification, overexpression and characterization of Chaperonin 10 homologues synthesized with and without N-terminal acetylation. J. Biol. Cliem. 270, 22037-22043.
279. Ryan, M. T., Herd, S. M., Sberna, G., Samuel, M. S., Hoogenraad, N. J., and Høj, P. B. (1996). The genes encoding mammalian Chaperonin 60 and Chaperonin 10 are linked heat-to-head and share a bidirectional promoter. Gene, in press.
280. Sadis, S., and Hightower, L. E. (1992). Unfolded proteins stimulate molecular chaperone hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry 31, 9406-9412.
281. Salvetti, M., Butinelli, C, Ristori, G., Carbonari, M., Cherchi, M., Fiorelli, M., Grazia Grasso, M., Toma, L., and Pozzilli, C. (1992). T-lymphocyte reactivity to the recombinant mycobacterial 65 and 70kDa heat shock proteins in multiple sclerosis. J. Autoimmtinity 5, 691-702.
282. Scherer, P. E., Krieg, U. C, Hwang, S. T., Vestweber, D., and Schatz, G. (1990). A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondria! stress protein. EMBO J. 9, 4315-4322
283. Scherer, P. E., Manning-Krieg, U. C., Jenö, P., Schatz, G., and Horst, M. (1992). Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane. Proc. Nati Acad. Sei. USA 89, 11930-11934.
284. Schett, G., Xu, Q., Amberger, A., Van der Zee, R., Reheis, H., Willeit, J., and Wick, G. (1995). Autoantibodies against heat shock protein 60 mediate endothelial cytotoxicity. /. Clin. Invest. 96, 2569-2577.
285. Schleyer, M., and Neupert, W. (1985). Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes. Cell 43,339-350.
286. Schleyer, M., Schmidt, B., and Neupert, W. (1982). Requirement of a membrane potential for the posttranslational transfer of proteins into mitochondria. Eur. J. Biochem. 125,109-116.
287. Schlossman, D. M., Schmid, S. L., Braell, W. A., and Rothman, J. E. (1984). An enzyme that removes clathrin coats: Purification of an uncoating ATPase. J. Cell Biol. 99, 723-733.
288. Schmid, D., Baici, A., Gehring, H., and Christen, P. (1994). Kinetics of molecular chaperone action. Science 263, 971-973.
289. Schmidt, M., and Buchner, J. (1992). Interaction of GroE with an all-β-protein. /. Biol. Cliem. 267, 16829-16833.
290. Schmitt, M., Neupert, W., and Langer, T. (1995). Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J. 14, 3434-3444.
291. Schnall, R., Mannhaupt, G., Stucka, R., Tauer, R., Ehnle, S., Schwarzlose, C., Vetter, L, and Feldmann, H. (1994). Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10, 1141-1155.
292. Schneider, H.-C., Berthold, J., Bauer, M. F., Dietmeier, K., Guiard, B., Brunner, M., and Neupert, W. (1994). Mitochondrial Hsp70/MIM44 complex facilitates protein import. Science 254, 1659-1662.
293. Schröder, H., Langer, T., Hartl, F.-U., and Bukau, B. (1993). DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144.
294. Seckler, R., and Jaenicke, R. (1992). Protein folding and protein refolding. FASEBJ. 6,2545-2552.
295. Segui-Real, B., Kispal, G., Lill, R., and Neupert, W. (1993). Functional independence of the protein translocation machineries in mitochondrial outer and inner membranes: Passage of preproteins through the intermembrane space. EMBO J. 12, 2211-2218.
296. Seki, N., Moczko, M., Nagase, T., Zufall, N., Ehmann, B., Dietmeier, K., Schäfer, E., Nomura, N., and Pfanner, N. (1995). A human homolog of the mitochondrial protein import receptor Moml9 can assemble with the yeast mitochondrial receptor complex. FEES Lett. 375, 307-310.
297. Selmaj, K., Brosnan, C. F., and Raine, C. S. (1991). Colocalization of lymphocytes bearing yS T-cell receptor and heat shock protein hsp 65+ oligodendrocytes in multiple sclerosis. Proc. Nail. Acad. Sei. USA. 88, 6452-6456.
298. Selmaj, K., Brosnan, CF., and Raine, C.S. (1992). Expression of heat shock protein-65 by oligodendrocytes in vivo and in vitro. Implications for multiple sclerosis. Neurology 42, 795-800.
299. Sheffield, W. P., Shore, G. C, and Randall, S. K. (1990). Mitochondria! precursor protein: Effects of 70-kilodalton heat shock protein on polypeptide folding, aggregation and import competence. J. Biol Chem. 265, 11069-11076.
300. Sherman, M. Y., and Goldberg, A. L. (1992). Involvement of the chaperone dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11, 71-77.
301. Shimokawa, T., and Fujimoto, H. (1996). Identification of a transciptional silencer in the protein coding region of the mouse major inducible Hsp70 gene. Biochem. Biophys. Res. Commun. 221, 843-848.
302. Simon, S. M., Peskin, C. S., and Oster, G. F. (1992). What drives the translocation of proteins? Proc. Nat!. Acad. Sei. USA 89, 3770-3774.
303. Smith, B. J., and Yaffe, M. P. (1991). A mutation in the yeast heat-shock factor gene causes temperature-sensitive defects in both mitochondrial protein import and the cell cycle. Mol. Cell Biol. 11, 2647-2655.
304. +1 locus. Genomics 15, 350-356.
305. Soltys, B. J., and Gupta, R. S. (1996). Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp. Cell Res. 222,16-27.
306. Sorger, P. K., and Pelham, H. R. B. (1987). Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells. EMBO J. 6, 993-998.
307. Squires, C., and Squires, C. L. (1992). The Clp proteins: Proteolysis regulators or molecular chaperones? /. Bacterial. 174, 1081-1085.
308. Srivastava, P. K. (1994). Heat shock proteins in immune response to cancer: The fourth paradigm. Experientia 50,1054-1060.
309. Stoller, G., Tradier, T., Rücknagel, P., Rahfeld, Jens-U., and Fischer, G. (1996). An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidylprolyl cis/trans isomerase activity. FEBS Lett. 384, 117-122.
310. Straus, D., Walter, W., and Gross, C. A. (1988). Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2, 1851-1858.
311. Suto, R., and Srivastava, P. K. (1995). A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 269, 1585-1588.
312. Suzuki, C. K., Suda, K., Wang, N., and Schatz, G. (1994). Requirement for the yeast gene LCWinintramitochondrial proteolysis and maintenance of respira lion. Science 264,273-276.
313. Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F. U. (1994). The ATP hydrolysis-dependent reaction cycle of the Eschericia coli Hsp70 system-DnaK, DnaJ, and GrpE. Proc N all Acad. Sei. USA 91, 10345-10349.
314. Szabo, A., Korzun, R., Hartl, F. U., and Flanagan, J. (1996). A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J. 15, 408-417.
315. Tauer, R., Mannhaupt, G., Schnall, R., Pajic, A., Langer, T., and Feldmann, H. (1994). YtalOp, a member of a novel ATPase family in yeast, is essential for mitochondrial function. FEBS Lett. 353, 197-200.
316. Thornton, K., Wang, Y., Weiner, H., and Gorenstein, D. G. (1993). Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase. /. Biol. Client. 268, 19906-19914.
317. +SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae. Mol. Cell. Biol. 13,5418-5426.
318. Tilly, K., Murialdo, H., and Georgopoulos, C. (1981). Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc. Nail. Acad. Sei. USA 78, 1629-1633.
319. Tisch, K., Yang, X-D., Singer, S. M., Liblau, R. S., Fugger, L., and McDevitt, H. O. (1993). Immune responses to glutamic acid decarboxylase correlates with insulitis in non-obese diabetic mice. Nature (London) 366, 72-75.
320. Todd, M. J., Viitanen, P. V., and Lorimer, G. H. (1993). Hydrolysis of adenosine 5′-triphosphate by Eschericia coli GroEL: Effects of GroES and potassium ion. Biochemistry 32,8560-8567.
321. Todd, M. J., Viita'nen, P. V., and Lorimer, G. H. (1994). Dynamics of the chaperonin ATPase cycle: Implications for facilitated folding. Science 265, 659-666.
322. 7 under protein folding conditions. Biochemistry 34, 14932-14941.
323. Todd, M. J., Lorimer, G. H., and Thirumalai, D. (1996). Chaperonin-facilitated protein folding: Optimisation of rate and yield by an iterative annealing mechanism. Proc. Nail. Acad. Sei. USA 93, 4030-4035.
324. 32. EMBO J. 14, 2551-2560.
325. Truscott, K. N., Høj, P. B., and Scopes, R. K. (1994). Purification and characterisation of chaperonin 60 and chaperonin 10 from the anaerobic thermophile Thermoanaerobacter brokii. Eur. J. Biochem. 222, 277-284.
326. Tsoulfa, G., Pook, G. A. W., van Embden, J. D. A., Young, D. B., Mehlert, A., Isenberg, D. A., Hay, F. C, and Lydyard, P. M. (1989). Raised serum IgG and IgA antibodies to mycobacterial antigens in rheumatoid arthritis. Ann. Rheum. Dis. 48, 118-123.
327. Ungermann, C, Neupert, V., and Cyr, D. M. (1994). The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science 266, 1250-1253.
328. Van Dyck, L., Pearce, D. A., and Sherman, F. (1994). PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 269, 238-242.
329. van Eden, W., Thole, J. E. R., van der Zee, E., Noordzij, A., van Embden, J. D. A., Hensen, E. J., and Cohen, I. R. (1988). Cloning of the mycobacterial epitope recognized by T lymphocytes in adjuvant arthritis. Nature {London) 331, 171-173.
330. Verner, K. (1993). Co-translational protein import into mitochondria: An alternative view. Trends Biochem. Sei. 18, 366-371.
331. Vestweber, D., Brunner, J., Baker, A., and Schatz, G. (1989). A 42K outer-membrane protein is a component of the yeast mitochondrial protein import site. Nature (London) 341,205-209.
332. Viitanen, P. V., Gatenby, A. A., and Lorimer, G. H. (1992a). Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sei. 1, 363-369.
333. Viitanen, P. V., Lorimer, G. H., Seetharam, R., Gupta, R. S., Oppenheim, J., Thomas, J. O., and Cowan, N. J. (1992b). Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. J. Biol. Chem. 267, 695-698.
334. von Ahsen, O., Voos, W., Henninger, H., and Pfanner, N. (1995). The mitochondrial protein import machinery: Role of ATP in dissociation of the Hsp70:Mim44 complex. /. Biol. Chem. 270, 29848-29853.
335. von Heijne, G. (1986). Mitochondrial targeting sequences form amphiphilic helices. EMBO J. 5, 1335-1342.
336. Voos, W., Gambill, D. B., Layloraya, S., Ang, D., Craig, E. A., and Pfanner, N. (1994). Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes. Mol. Cell. Biol. 14, 6627-6634.
337. Voos, W., von Ahsen, O., Müller, H., Guiard, B., Rassow, J., and Pfanner, N. (1996). Differential requirement for the mitochondrial hsp70-Tim44 complex in unfolding and translocation of preproteins. EMBO J. 15, 2668-2677.
338. Wagner, I., Arlt, H., van Dyck, L., Langer, T., and Neupert, W. (1994). Molecular chaperones cooperate with PIMl protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13, 5135-5145.
339. Waltner, M., and Weiner, H. (1995). Conversion of a non processed mitochondrial precursor protein into one that is processed by the mitochondrial processing peptidase. /. Biol. Chem. 270,26311-26317.
340. Wand-Wiirttenberger, A., Schoel, B., Ivanyi, J., and Kaufmann, S.H.E. (1991). Surface expression by mononuclear phagocytes of an epitope shared with mycobacerial heat shock protein 60. Eur. J. Immiuwl. 21, 1089-1092.
341. Wang, N., Gottesman, S., Willingham, M. C, Gottesman, M. M., and Maurizi, M. R. (1993). A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc. Natl. Acad. Sei. USA 90, 11247-11251.
342. Wang, N., Maurizi, M. R., Emmert-Buck, L., and Gottesman, M. M. (1994). Synthesis, processing, and localisation of human Lon protease. /. Biol. Chem. 269, 29308-29313.
343. Watabe, S., and Kimura, T. (1985a). ATP-dependent protease in bovine adrenal cortex. J. Biol. Client. 260, 5511-5517.
344. Watabe, S., and Kimura, T. (1985b). Adrenal cortex mitochondrial enzyme with ATP-dependent protease and protein-dependent ATPase activities. /. Biol. Chem. 260, 14498-14504.
345. Wawrzynów, A., and Zylicz, M. (1995). Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. J. Biol. Chem. 270, 19300-19306.
346. Wawrzynów, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Johsen, M., Graves, B., Georgopoulos, C., and Zylicz, M. (1995). The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14, 1867-1877.
347. Webster, T. J., Naylor, D. J., Hartman, D. J., Höj, P. B., and Hoogenraad, N. J. (1994). cDNA cloning and efficient mitochondrial import of pre-mtHSP70 from rat liver. DNA Cell Biol. 13, 1213-1220.
348. Weissman, J. S., Kashi, Y., Fenton, W. A., and Horwich, A. L. (1994). GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78, 693-702.
349. Weissman, J. S., Hohl, C. M., Kovalenko, O., Kashi, Y., Chen, S., Braig, K., Saibil, H. R., Fenton, W. A., and Horwich, A. L. (1995). Mechanism of GroEL-action: Productive release of polypeptide from a sequestered position under GroES. Cell 83, 577-587.
350. Weissman, J. S., Rye, H. S., Fenton, W. A., Beechem, J. M., and Horwich, A. L. (1996). Characterisation of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490.
351. Welch, W. J. (1990). The mammalian stress response: Cell physiology and biochemistry of stress proteins. In "Stress Proteins in Biology and Medicine" (R. I., Morimoto, A. Tissières, and C. Georgopoulos, Eds.), pp. 223-278. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
352. Welch, W. J., and Feramisco, J. R. (1985). Rapid purification of mammalian 70,000-dalton stress proteins: Affinity of the proteins for nucleotides. Mol. Cell. Dial. 5, 1229-1237.
353. Werner-Washburne, M., Stone, D. E. and Craig, E. A. (1987). Complex interactions among members of an essential subfamily of Itsp70 genes in Saccharoniyces cerevisiae. Mot. Cell. Biol. 7, 2568-2577.
354. Westerman, B., Pripp-Buus, C, Neupert, W., and Schwarz, E. (1995). The role of the GrpE homologue, Mgelp, in mediating protein import and protein folding in mitochondria. EMBO J. 14, 3452-3460.
355. Westwood, J. T., Clos, J., and Wu, C. (1991). Stress-induced oligomerization and chromosomal relocalization of heat-shock factor. Nature (London) 353, 822-827.
356. Wetzel, I. R. (1994). Mutations and off-pathway aggregation of proteins. Trends Bioteclmol. 12, 193-198.
357. Wickner, R. B. (1994). [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharamyces cerevisiae. Science 264, 566-569.
358. Wickner, S., Gottesman, S., Skowyra, D., Hoskins, J., McKenney, K., and Maurizi, M. R. (1994). A molecular chaperone, ClpA functions like DnaK and DnaJ. Proc. Nail. Acad. Sei. USA 91, 12218-12222.
359. Wiedmann, B., Sakai, H., Davis, T. A., and Wiedmann, M. (1994). A protein complex required for signal-sequence-specific sorting and translocation. Nature (London) 370, 434-440.
360. Witte, C, Jensen, R. E., Yaffe, M. P., and Schatz, G. (1988). MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease. EMBO J. 7, 1439-1447.
361. Wojtkowiak, D., Georgopoulos, C., and Zylicz, M. (1993). Isolation and characterisation of ClpX, a new ATP-dependent specificity component of the Clp protease of Escliericliia coll. J. Biol. Chem. 268, 22609-22617.
362. Wu, C, Clos, J., Giorgi, G., Haroun, R. I., Kirn, S-J., Rabindran, S. K., Westwood, J. T., Wisniewski, J., and Yim, G. (1994). Structure and regulation of heat shock transcription factor. In "The Biology of Heat Shock Proteins and Molecular Chaperones" (R. I., Morimoto, A. Tissières, and C. Georgopoulos, Eds.), pp. 395-416. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
363. Wiicherpfenning, K. W., Newcombe, J., Li, H., Keddy, L., Cuzner, M. L., and Hafler, D. A. (1992). ylB T-cell reperoire in acute multiple sclerosis lesions. Proc. Natl. Acad. Sei. USA 89, 4588-4592.
364. Xu, Q., Schett, G., Seitz, C. S., Hu, Y., Gupta, R. S., and Wick, G. (1994). Surface staining and cytotoxic activity of heat-shock protein 60 antibody in stressed aortic endothelical cells. Circ. Res. 75, 1078-1085.
365. Yang, M., Jensen, R. E., Yaffe, M. P., Oppliger, W., and Schatz, G. (19S8). Import of proteins into yeast mitochondria: The purified matrix processing protease contains two subunits which are encoded by the nuclear MASl and MAS2 genes. EMBO J. 7, 3857-3862.
366. Young, R.A. (1990). Stress proteins and immunology. Annn. Rev. Immunol 8, 401-420.
367. Zhong, T., and Arndt, K. T. (1993). The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of translation. Cell 73, 1175-1186.
368. Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., and Hendrickson, W. A. (1996). Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614.
369. Ziegelhoffer, T., Lopez-Buesa, P., and Craig, E. A. (1995). The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydjlp and peptide substrates. J. Biol. Chem. 270, 10412-10419.
370. Zylicz, M., and Georgopoulos, C. (1984). Purification and properties of the Escliericia coli dnaK replication protein. J. Biol. Chem. 259, 8820-8825.