Synergistic roles of Hs1VU and other ATP-dependent proteases in controlling in vivo turnover of σ32 and abnormal proteins in Escherichia coli

Journal of Bacteriology

Volumn 179, Issue 23, 1997, Pages 7219-7225

  Kanemori, Masaaki ^a   Nishihara, Kazuyo ^a   Yanagi, Hideki ^a   Yura, Takashi ^a  

^a Kyoto Research Park   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HEAT SHOCK PROTEIN; PROTEINASE; PROUROKINASE; SIGMA FACTOR; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; BACTERIAL PROTEIN; CLPXP PROTEASE, E COLI; ENDOPEPTIDASE CLP; ENDOPEPTIDASE LA; ESCHERICHIA COLI PROTEIN; FTSH PROTEIN, BACTERIA; FTSH PROTEIN, E COLI; HEAT SHOCK SIGMA FACTOR 32; HEAT-SHOCK SIGMA FACTOR 32; LON PROTEIN, E COLI; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; SARUPLASE; SERINE PROTEINASE; TRANSCRIPTION FACTOR; UROKINASE;

ARTICLE; BACTERIAL GROWTH; CONTROLLED STUDY; ESCHERICHIA COLI; GENE DELETION; GENE MUTATION; HEAT SHOCK RESPONSE; NONHUMAN; OPERON; PLASMID; PRIORITY JOURNAL; PROTEIN METABOLISM; PROTEIN SYNTHESIS; TEMPERATURE SENSITIVITY; BACTERIAL GENE; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; MUTATION;

ADENOSINE TRIPHOSPHATASES; ATP-DEPENDENT PROTEASES; BACTERIAL PROTEINS; ENDOPEPTIDASE CLP; ENDOPEPTIDASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE DELETION; GENES, BACTERIAL; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; HUMANS; MEMBRANE PROTEINS; MUTATION; PROTEASE LA; RECOMBINANT PROTEINS; SERINE ENDOPEPTIDASES; SIGMA FACTOR; TRANSCRIPTION FACTORS; URINARY PLASMINOGEN ACTIVATOR;

EID: 0030613795     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.23.7219-7225.1997     Document Type: Article

References (45)

1. Akiyama, Y., T. Ogura, and K. Ito. 1994. Involvement of FtsH in protein assembly into and through the membrane. J. Biol. Chem. 269:5218-5224.
2. Bukau, B. 1993. Regulation of the Escherichia coli heat-shock response. Mol. Microbiol. 9:671-680.
3. Chuang, S.-E., V. Burland, G. Plunkett III, D. L. Daniels, and F. R. Blattner. 1993. Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene 134:1-6.
4. Craig, E. A., and C. A. Gross. 1991. Is hsp70 the cellular thermometer? Trends Biochem. Sci. 16:135-140.
5. 32. Cell 69:833-842.
6. Georgopoulos, C., K. Liberek, M. Zylicz, and D. Ang. 1994. Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response, p. 209-249. In R. I. Morimoto, A. Tissières, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
7. Goff, S. A., and A. L. Goldberg. 1985. Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes. Cell 41:587-595.
8. Goldberg, A. L. 1992. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur. J. Biochem. 203:9-23.
9. Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
10. Gottesman, S., and M. R. Maurizi. 1992. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56:595-621.
11. Gross, C. A. 1996. Function and regulation of the heat shock proteins, p. 1382-1399. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. ASM Press, Washington, D.C.
12. Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-580.
13. 32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc. Natl. Acad. Sci. USA 92:3516-3520.
14. Huang, H. C., and A. L. Goldberg. Personal communication.
15. Ito, K., Y. Akiyama, T. Yura, and K. Shiba. 1986. Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiology. J. Bacteriol. 167:201-204.
16. Kanemori, M. Unpublished data.
17. 32 in Escherichia coli. J. Bacteriol. 176:5648-5653.
18. Kessel, M., W. 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.
19. Kitagawa, M. Unpublished data.
20. 32 transcription factor. Proc. Natl. Acad. Sci. USA 89:3516-3520.
21. Lupas, A., P. Zwickl, and W. Baumeister. 1994. Proteasome sequences in eubacteria. Trends Biochem. Sci. 19:533-534.
22. Maurizi, M. R. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48:178-201.
23. Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
24. Missiakas, D., F. Schwager, J.-M. Betton, C. Georgopoulos, and S. Raina. 1996. Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15:6899-6909.
25. 32 synthesis during the heat shock response of Escherichia coli. Proc. Natl. Acad. Sci. USA 88:10515-10519.
26. Oeura, T. Personal communication.
27. Parsell, D. A., and R. T. Sauer. 1989. Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes Dev. 3:1226-1232.
28. Qu, J.-N., S. Makino, H. Adachi, Y. Koyama, Y. Akiyama, K. Ito, T. Tomoyasu, T. Ogura, and H. Matsuzawa. 1996. The tolZ gene of Escherichia coli is identified as the ftsH gene. J. Bacteriol. 178:3457-3461.
29. 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. USA 93:5808-5813.
30. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
31. Shirai, Y., Y. Akiyama, and K. Ito. 1996. Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones. J. Bacteriol. 178:1141-1145.
32. Stahl, F. W., I. Kobayashi, D. Thaler, and M. M. Stahl. 1986. Direction of travel of RecBC recombinase through bacteriophage lambda DNA. Genetics 113:215-227.
33. 32. Nature (London) 329:348-351.
34. 32. Genes Dev. 4:2202-2209.
35. Tilly, K., N. McKittrick, M. Zylicz, and C. Georgopoulos. 1983. The dnaK protein modulates the heat-shock response of Escherichia coli. Cell 34:641-646.
36. Tobe, T., K. Ito, and T. Yura. 1984. Isolation and physical mapping of temperature-sensitive mutants defective in heat-shock induction of proteins in Escherichia coli. Mol. Gen. Genet. 195:10-16.
37. 32. EMBO J. 14:2551-2560.
38. Wawrzynow, A., D. Wojtkowiak, J. Marszalek, 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.
39. Wild, J., W. A. Walter, C. A. Gross, and E. Altman. 1993. Accumulation of secretory protein precursors in Escherichia coli induces the heat shock response. J. Bacteriol. 175:3992-3997.
40. Yano, R., M. Imai, and T. Yura. 1987. The use of operon fusions in studies of the heat-shock response: effects of altered sigma32 on heat-shock promoter function in Escherichia coli. Mol. Gen. Genet. 207:24-28.
41. 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli. J. Bacteriol. 172:2124-2130.
42. Yoo, S. J., J. H. Seol, D. H. Shin, M. Rohrwild, M.-S. Kang, K. Tanaka, A. L. Goldberg, and C. H. Chung. 1996. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J. Biol. Chem. 271:14035-14040.
43. 32. Genes Cells 1:277-284.
44. Yura, T., H. Nagai, and H. Mori. 1993. Regulation of heat shock response in bacteria. Annu. Rev. Microbiol. 47:321-350.
45. 32 synthesis mediated by mRNA secondary structure: a primary step of the heat shock response in Escherichia coli. Nucleic Acids Res. 21:5449-5455.