Protein quality control: Triage by chaperones and proteases

Genes and Development

Volumn 11, Issue 7, 1997, Pages 815-823

  Gottesman, Susan ^a   Wickner, Sue ^a   Maurizi, Michael R ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEINASE;

ENZYME ACTIVITY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SYNTHESIS REGULATION; REGULATORY MECHANISM; REVIEW;

EID: 0030936847     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.11.7.815     Document Type: Review

References (69)

1. Akiyama, Y., T. Ogura, and K. Ito. 1994. Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter. J. Biol. Chem. 269: 5218-5224.
2. Akiyama, Y., A. Kihara, H. Tokuda, and K. Ito. 1996. FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J. Biol. Chem. 271: 31196-31201.
3. Arlt, H., R. Tauer, H. Feldmann, W. Neupert, and T. Langer. 1996. The Yta10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85: 875-885.
4. Baker, T.A., A.D. Grossman, and C.A. Gross. 1984. A gene regulating the heat shock response in E. coli affects proteolysis. Proc. Natl. Acad. Sci. 81: 6779-6783.
5. Bukau, B. and G.C. Walker. 1989. ΔdnaK52 mutants of Escherichia coli have defects in segregation and plasmid maintenance at normal temperatures. J. Bacteriol. 171: 6030-6038.
6. +]. Science 268: 881-884.
7. Goff, S.A., L.P. Casson, and A.L. Goldberg. 1984. Heat shock regulatory gene htpR influences rates of protein degradation and expression of the lon gene in Escherichia coli. Proc. Natl. Acad. Sci. 81: 6647-6651.
8. Goldberg, A., R.P. Morschell, C.H. Chung, and M.R. Maurizi. 1994. ATP-dependent protease La (lon) from Escherichia coli. Methods Enzymol. 244: 350-375.
9. Gottesman, S. 1989. Genetics of proteolysis in Escherichia coli. Annu. Rev. Genet. 23: 163-198.
10. _. 1996a. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30: 465-506.
11. _. 1996b. Roles for energy-dependent proteases in regulatory cascades. In Regulation of gene expression in Escherichia coli, (ed. E.C.C. Lin and A.S. Lynch) pp. 503-519. R.G. Landes Co., Austin, TX.
12. Gottesman, S. and M.R. Maurizi. 1992. Regulation by proteolysis: Energy-dependent proteases and their targets. Microbiol. Rev. 56: 592-621.
13. Gottesman, S., W.P. Clark, V. de Crecy-Lagard, and M.R. Maurizi. 1993. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. J. Biol. Chem. 268: 22618-22626.
14. Gragerov, A., E. Nudler, N. Komissarova, G.A. Gaitanaris, M.E. Gottesman, and V. Nikiforov. 1992. Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc. Natl. Acad. Sci. 89: 10341-10344.
15. Gross, C. 1996. Function and regulation of the heat shock proteins. In Escherichia coli and Salmonella typhimurium (ed. F.C. Neidhardt, R. Curtiss III, J.L. Ingraham, E.C.C. Lin, J.K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter and H.E. Umbarger), pp. 1382-1399. American Society for Microbiology, Washington, D.C.
16. Guzelin, E., M. Rep, and L.A. Grivell. 1996. Afg3p, a mitochondrial ATP-dependent metalloprotease, is involved in degradation of mitochondrially-encoded Cox1, Cox3, Cob, Su6, Su8 and Su9 subunits of the inner membrane complexes III, IV and V. FEBS Lett. 381: 42-46.
17. Herman, C., D. Thévenet, R. D'Ari, and P. Bouloc. 1995. Degradation of σ32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc. Natl. Acad. Sci. 92: 3516-3520.
18. Horwich, A.L. 1995. Resurrection or destruction. Curr. Biol. 5: 455-458.
19. Jubete, Y., M.R. Maurizi, and S. Gottesman. 1996. Role of the heat shock protein DnaJ in the Lon-dependent degradation of naturally unstable proteins. J. Biol. Chem. 271: 30798-30803.
20. Kandror, O., L. Busconi, M. Sherman, and A.L. Goldberg. 1994. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J. Biol Chem. 269: 23575-23582.
21. Kandror, O., M. Sherman, M. Rhode, and A.L. Goldberg. 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.
22. Keller, J.A. and L.D. Simon. 1988. Divergent effects of a dnaK mutation on abnormal protein degradation in Escherichia coli. Mol. Microbiol. 2: 31-41.
23. Kessel, M., M.R. Maurizi, B. Kim, E. Kocsis, B.L. Trus, S.K. Singh, and A.C. Steven. 1995. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26S proteasome. J. Mol. Biol. 250: 587-594.
24. Kessel, M., W.-F. Wu, S. Gottesman, E. Kocsis, A.C. Steven, and M.R. Maurizi. 1996. Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 398: 274-278.
25. Kihara, A., Y. Akiyama, and K. Ito. 1995. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. 92: 4532-4536.
26. Kroh, H.E. and L.D. Simon. 1991. Increased ATP-dependent proteolytic activity in Lon-deficient Escherichia coli strains lacking the DnaK protein. J. Bacteriol. 173: 2691-2695.
27. Kruklitis, R., D.J. Welty, and H. Nakai. 1996. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15: 935-944.
28. LaRossa, R.A. and T.K. Van Dyk. 1991. Physiological roles of the DnaK and GroE stress proteins: Catalysts of protein folding or macromolecular sponges? Mol. Microbiol. 5: 529-534.
29. Langer, T. and W. Neupert. 1996. Regulated protein degradation in mitochondria. Experientia 52: 1069-1076.
30. Lee, D.H., M.Y. Sherman, and A.L. Goldberg. 1996. Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae. Molec. Cell. Biol. 16: 4773-4781.
31. Levchenko, I., L. Luo, and T.A. Baker. 1995. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes & Dev. 9: 2399-2408.
32. Maurizi, M.R. 1987. Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli. J. Biol. Chem. 262: 2696-2703.
33. _. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48: 178-201.
34. Maurizi, M.R., S. Wickner, and S. Gottesman. 1997. Chaperones and charonins: Protein unfolding enzymes and proteolysis. In Molecular biology of chaperones and protein catalysts (ed. B. Bukau), Harwood Academic Publishers, Amsterdam, The Netherlands. (In Press).
35. Mhammedi-Alaoui, A., M. Pato, M.-J. Gamma, and A. Toussaint. 1994. A new component of bacteriophage Mu replicative transposition machinery: The Escherichia coli ClpX protein. Mol. Microbiol. 11: 1109-1116.
36. Missiakas, D., F. Schwager, J.-M. Betton, C. Georgopoulos, and S. Raina. 1996. Isolation and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in E. coli. EMBO J. 15: 6899-6909.
37. Moczko, M., B. Schonfisch, W. Voos, N. Pfanner, and J. Rassow. 1995. The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J. Mol. Biol. 254: 538-543.
38. Pajic, A., R. Tauer, H. Feldmann, W. Neupert, and T. Langer. 1994. Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. FEBS Lett. 353: 201-206.
39. Pak, M. and S. Wickner. 1997. Mechanism of protein remodeling by ClpA chaperone. Proc. Natl. Acad. Sci. 94: (in press).
40. Parsell, D.A., A.S. Kowal, M.A. Singer, and S. Lindquist. 1994. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372: 475-478.
41. Rep, M., J.M. van Dijl, K. Suda, G. Schatz, L.A. Grivell, and C.K. Suzuki. 1996. Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon. Science 274: 103-106.
42. Rohrwild, M., O. Coux, H.-C. Huang, R.P. Moerschell, S.J. Yoo, J.H. Seol, C.H. Chung, and A.L. Goldberg. 1996. HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc. Natl. Acad. Sci. 93: 5808-5813.
43. Sanchez, Y., D.A. Parsell, J. Taulien, J.L. Vogel, E.A. Craig, and S. Lindquist. 1993. Genetic evidence for a functional relationship between Hsp104 and Hsp70. J. Bacteriol 175: 6484-6491.
44. Sanchez, Y., J. Taulien, K.A. Borkovich, and S. Lindquist. 1992. Hsp104 is required for tolerance to many forms of stress. EMBO J. 11: 2357-2364.
45. Schirmer, E.C., J.R. Glover, M.A. Singer, and S. Lindquist. 1996. HSP100/Clp proteins: A common mechanism explains diverse functions. Trends Biochem. Sci. 21: 289-296.
46. Schmitt, M., W. Neupert, and T. Langer. 1995. Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J. 14: 3434-3444.
47. Schneider, C., L. Sepp-Lorenzino, E. Nimmesgern, O. Ouerfelli, S. Danishefsky, N. Rosen, and F.U. Hartl. 1996. Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. 93: 14536-14541.
48. Sherman, M.Y. and A.L. Goldberg. 1991. Formation in vitro of complexes between an abnormal fusion protein and the heat shock proteins from Escherichia coli and yeast mitochondria. J. Bacteriol. 173: 7249-7256.
49. _. 1992. Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11: 71-77.
50. Shirai, Y., Y. Akiyama, and K. Ito. 1996. Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones. J. Bacteriol 178: 1141-1145.
51. Sonezaki, S., Y. Ishii, K. Okita, T. Sugino, A. Kondo, and Y. Kato. 1995. Overproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitro. Appl. Microbiol. Biotechnol. 43: 304-309.
52. Squires, C.L., S. Pedersen, B.M. Ross, and C. Squires. 1991. ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173: 4254-4262.
53. Straus, D.B., W.A. Walter, and C. Gross. 1988. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes & Dev. 2: 1851-1858.
54. Suzuki, C.K., K. Suda, N. Wang, and G. Schatz. 1994. Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 264: 273-276.
55. Tauer, R., G. Mannhaupt, R. Schnall, A. Pajic, T. Langer, and H. Feldmann. 1994. Yta10p, a member of a novel ATPase family in yeast, is essential for mitochondrial function. FEBS Lett. 353: 197-200.
56. Thompson, M.W. and M.R. Maurizi. 1994. Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. J. Biol. Chem. 269: 18201-18208.
57. Tilly, K. and M. Yarmolinsky. 1989. Participation of Escherichia coli heat shock proteins DnaJ, DnaK, and GrpE in Pl plasmid repression. J. Bacteriol. 171: 6025-6029.
58. Tomoyasu, T., T. Yuki, S. Morimura, H. Mori, K. Yamanaka, H. Niki, S. Hiraga, and T. Ogura. 1993. The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression. J. Bacteriol. 175: 1344-1351.
59. 32. EMBO J. 14: 2551-2560.
60. van Melderen, L., M.H.D. Thi, P. Lecchi, S. Gottesman, M. Couturier, and M.R. Maurizi. 1996. ATP-dependent degradation of CcdA by Lon protease: Effects of secondary structure and heterologous subunit interactions. J. Biol. Chem. 271: 27730-27738.
61. Vogel, J.L., D.A. Parsell, and S. Lindquist. 1995. Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation. Curr. Biol. 5: 306-317.
62. Wagner, I., H. Arlt, L. Van Dyck, T. Langer, and W. Neupert. 1994. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13: 5135-5145.
63. Wawrzynow, A., D. Wojtkowiak, J. Marzsalek, B. Banecki, M. Jonsen, B. Graves, C. Georgopoulos, and M. Zylicz. 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.
64. Wawrzynow, A., B. Banecki, and M. Zylicz. 1996. The Clp ATPases define a novel class of molecular chaperones. Mol. Microbiol. 21: 895-899.
65. Waxman, L. and A.L. Goldberg. 1986. Selectivity of intracellular proteolysis: Protein substrates activate the ATP-dependent protease (La). Science 232: 500-503.
66. Wickner, S., J. Hoskins, and K. McKenney. 1991. Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin. Proc. Natl. Acad. Sci. 88: 7903-7907.
67. Wickner, S., D. Skowyra, J. Hoskins, and K. McKenney. 1992. DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step. Proc. Natl. Acad. Sci. 89: 10345-10349.
68. Wickner, S., S. Gottesman, D. Skowyra, J. Hoskins, K. McKenney, and M.R. Maurizi. 1994. A molecular chaperone, ClpA, functions like DnaK and DnaJ. Proc. Natl. Acad. Sci. 91: 12218-12222.
69. Wojtkowiak, D., C. Georgopoulos, and M. Zylicz. 1993. ClpX, a new specificity component of the ATP-dependent Escherichia coli Clp protease, is potentially involved in X DNA replication. J. Biol. Chem. 268: 22609-22617.