A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein

Cell

Volumn 97, Issue 3, 1999, Pages 339-347

  Spiess, Christoph ^a   Beil, Alexandra ^a   Ehrmann, Michael ^a  

^a UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; PROTEINASE;

ARTICLE; ENZYME ANALYSIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN METABOLISM; PROTEIN MODIFICATION; STRESS; TEMPERATURE DEPENDENCE;

EID: 0033617146     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80743-6     Document Type: Article

References (42)

1. Arslan, E., Schulz, H., Zufferey, R., Kunzler, P., and Thony-Meyer, L. (1998). Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli. Biochem. Biophys. Res. Commun. 257, 744-747.
2. Baneyx, F., and Georgiou, G. (1991). Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo. J. Bacteriol. 173, 2696-2703.
3. Bardwell, J.C., McGovern, K., and Beckwith, J. (1991). Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589.
4. Betton, J.-M., Sassoon, N., Hofnung, M., and Laurent, M. (1998). Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli. J. Biol. Chem. 273, 8897-8902.
5. Buchner, J., Grallert, H., and Jakob, U. (1998). Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 290, 323-338.
6. Bukau, B., and Horwich, A. (1998). The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366.
7. Cavard, D. (1995). Role of DegP protease on levels of various forms of colicin A lysis protein. FEMS Microbiol. Lett. 125, 173-178.
8. Chang, A.C.Y., and Cohen, S.N. (1978). Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134, 1141-1156.
9. Danese, P., Snyder, W., Cosma, C., Davis, L., and Silhavy, T. (1995). The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stressinducible periplasmic protease, DegP. Genes Dev. 9, 387-398.
10. Dong, J., luchi, S., Kwan, H., Lu, Z., and Lin, E. (1993). The deduced amino acid sequence of the cloned cpxRgene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli. Gene 136, 227-230.
11. Freundlieb, S., and Boos, W. (1986). α-Amylase of Escherichia coli, mapping and cloning of the structural gene, mals, and identification of its product as a periplasmic protein. J. Biol. Chem. 267, 2946-2953.
12. Glover, J., and Lindquist, S. (1998). Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82.
13. Gottesman, S. (1996). Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30, 465-506.
14. Gottesman, S., Wickner, S., and Maurizi, M. (1997). Protein quality control: triage by chaperones and proteases. Genes Dev. 11, 815-823.
15. Guigueno, A., Belin, P., and Boquet, P. (1997). Defective export in Escherichia coli caused by DsbA'-PhoA hybrid proteins whose DsbA' domain cannot fold into a conformation resistant to periplasmic proteases. J. Bacteriol. 179, 3260-3269.
16. BAD promoter. J. Bacteriol. 177, 4121-4130.
17. Hu, S., Carozza, M., Klein, M., Nantermet, P., Luk, D., and Crowl, R. (1998). Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage. J. Biol. Chem. 273, 34406-34412.
18. Kihara, A., and Ito, K. (1998). Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences. J. Biol. Chem. 273, 29770-29775.
19. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
20. Levchenko, I., Smith, C., Walsh, N., Sauer, R., and Baker, T. (1997). PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91, 939-947.
21. Lindquist, S., and Craig, E. (1988). The heat-shock proteins. Annu. Rev. Genet. 22, 631-677.
22. Lipinska, B., Sharma, S., and Georgopoulos, C. (1988). Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription. Nucleic Acids Res. 16, 10053-10067.
23. Miller, J. (1972). Experiments in Molecular Genetics (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory).
24. Missiakas, D., and Raina, S. (1998). The extracytoplasmic function sigma factors: role and regulation. Mol. Microbiol. 28, 1059-1066.
25. Neu, H., and Heppel, L. (1965). The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240, 3685-3692.
26. Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988). Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie brilliant blue G-250 and R-250. Electrophoresis 9, 255-262.
27. Nichtl, A., Buchner, J., Jaenicke, R., Rudolph, R., and Scheibel, T. (1998). Folding and association of β-galactosidase. J. Mol. Biol. 282, 1083-1091.
28. Pallen, M., and Wren, B. (1997). The HtrA family of serine proteases. Mol. Microbiol. 26, 209-221.
29. Pogliano, J., Lynch, A., Belin, D., Lin, E., and Beckwith, J. (1997). Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev. 11, 1169-1182.
30. Prinz, W.A., Spiess, C., Ehrmann, M., Schierle, C., and Beckwith, J. (1996). Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase. EM BO J. 15, 5209-5217.
31. Rawlings, N., and Barrett, A. (1994). Families of serine peptidases. Methods Enzymol. 244, 19-61.
32. Savel'ev, A., Novikova, L., Kovaleva, I., Luzikov, V., Neupert, W., and Langer, T. (1998). ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system. J. Biol. Chem. 273, 20596-20602.
33. Schneider, E., Freundlieb, S., Tapio, S., and Boos, W. (1992). Molecular characterization of the Mali-dependent periplasmic alpha-amylase of Escherichia coli encoded by mais. J. Biol. Chem. 267, 5148-5154.
34. Skorko-Glonek, J., Krzewski, K., Lipinska, B., Bertoli, E., and Tanfani, F. (1995). Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study. J. Biol. Chem. 270, 11140-11146.
35. Snyder, W., and Silhavy, T. (1995). Beta-galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli. J. Bacteriol. 177, 953-963.
36. Sone, M., Kishigami, S., Yoshihisa, T., and Ito, K. (1997). Roles of disulfide bonds in bacterial alkaline phosphatase. J. Biol. Chem. 272, 6174-6178.
37. Spiess, C., Happersberger, H.P., Glocker, M.O., Spiess, E., Rippe, K., and Ehrmann, M. (1997). Biochemical characterization and mass spectrometric disulfide bond mapping of periplasmic α-amylase MalS of Escherichia coli. J. Biol. Chem. 272, 22125-22133.
38. St Geme, J.W., III, and Grass, S. (1998). Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins. Mol. Microbiol. 27, 617-630.
39. Strauch, K.L., and Beckwith, J. (1988). An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. USA 85, 1576-1580.
40. Suzuki, C., Rep, M., van Dijl, J., Suda, K., Grivell, L., and Schatz, G. (1997). ATP-dependent proteases that also chaperone protein biogenesis. Trends Biochem. Sci. 22, 118-123.
41. Waller, P., and Sauer, R. (1996). Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol. 778, 1146-1153.
42. Zumbrunn, J., and Trueb, B. (1996). Primary structure of a putative serine protease specific for IGF-binding proteins. FEBS Lett. 398, 187-192.