Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin

Journal of Bacteriology

Volumn 179, Issue 21, 1997, Pages 6602-6608

  Rietsch, Arne ^a   Bessette, Paul ^b   Georgiou, George ^b   Beckwith, Jonathan ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b The University of Texas at Austin   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOPLASM PROTEIN; ISOMERASE; MEMBRANE PROTEIN; THIOREDOXIN; THIOREDOXIN REDUCTASE;

ARTICLE; CYTOPLASM; DISULFIDE BOND; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GRAM NEGATIVE BACTERIUM; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0030668672     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.21.6602-6608.1997     Document Type: Article

References (43)

1. Anfinsen, C. B. 1973. Principles that govern the folding of protein chains. Science 181:223-230.
2. Bachmann, B. J. 1990. Linkage map of Escherichia coli K-12, edition 8. Microbiol. Rev. 54:129-197.
3. Bardwell, J. C., J. O. Lee, G. Jander, N. Martin, D. Belin, and J. Beckwith. 1993. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA 90:1038-1042.
4. Bardwell, J. C., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589.
5. Belin, D., J.-D. Vassalli, C. Combepine, F. Godea, Y. Nagamine, E. Kocher, and R. M. Duvoisin. 1985. Cloning, nucleotide sequence and expression of cDNAs encoding mouse urokinase-type plasminogen activator. Eur. J. Biochem. 148:225-232.
6. Boyd, D., C. Manoil, and J. Beckwith. 1987. Determinants of membrane protein topology. Proc. Natl. Acad. Sci. USA 84:8525-8529.
7. Chivers, P. T., M. C. A. Laboissière, and R. T. Raines. 1996. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 15:2659-2667.
8. Creighton, T. E., D. A. Hillson, and R. B. Freedman. 1980. Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds. J. Mol. Biol. 142:43-62.
9. Crooke, H., and J. Cole. 1995. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase domain. Mol. Microbiol. 15:1139-1150.
10. Derman, A. I., W. A. Prinz, D. Belin, and J. Beckwith. 1993. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262:1744-1747.
11. Duvoisin, R. M., D. Belin, and H. M. Kirsch. 1986. A plasmid expression vector that permits stabilization of both mRNAs and proteins encoded by the cloned genes. Gene 45:193-201.
12. Gilbert, H. F. 1990. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. 63:69-172.
13. Goldenberg, D. P. 1988. Kinetic analysis of the folding and unfolding of a mutant form of bovine pancreatic trypsin inhibitor lacking the cysteine-14 and -38 thiols. Biochemistry 27:2481-2489.
14. Guilhot, C., G. Jander, N. L. Martin, and J. Beckwith. 1995. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. USA 92:9895-9899.
15. BAD promoter. J. Bacteriol. 177:4121-4130.
16. Holmgren, A. 1989. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:13963-13966.
17. Holmgren, A., and F. Åslund. 1995. Glutaredoxin. Methods Enzymol. 252: 283-292.
18. Holmgren, A., and M. Björnstedt. 1995. Thioredoxin and thioredoxin reductase. Methods Enzymol. 252:199-208.
19. Hu, C.-H., and C.-L. Tsou. 1991. Formation of enzyme-substrate disulfide linkage during catalysis by protein disulfide isomerase. FEBS Lett. 290:87-89.
20. Kamitami, S., Y. Akiyama, and K. Ito. 1992. Identification and characterization of an Escherichia coli gene required for correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11:57-62.
21. Kishigami, S., E. Kanaya, M. Kikuchi, and K. Ito. 1995. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J. Biol. Chem. 270:17072-17074.
22. Laboissière, M. C., S. L. Sturley, and R. T. Raines. 1995. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270:28006-28009.
23. LaMantia, M. L., and W. J. Lennarz. 1993. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74:899-908.
24. Lovett, S. T., and R. D. Kolodner. 1991. Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of RecJ-overexpression plasmids. J. Bacteriol. 173:353-364.
25. Martin, J. L., J. C. Bardwell, and J. Kuriyan. 1993. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365: 464-468.
26. Missiakas, D., C. Georgopoulos, and S. Raina. 1993. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc. Natl. Acad. Sci. USA 90:7084-7088.
27. Missiakas, D., C. Georgopoulos, and S. Raina. 1994. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13:2013-2020.
28. Missiakas, D., F. Schwager, and S. Raina. 1995. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14:3415-3424.
29. Ostermeier, M., K. De Sutter, and G. Georgiou. 1996. Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds. J. Biol. Chem. 271:10616-10622.
30. Ostermeier, M., and G. Georgiou. 1994. The folding of bovine pancreatic trypsin inhibitor in the Escherichia coli periplasm. J. Biol. Chem. 269:21072-21077.
31. Rietsch, A., D. Belin, N. Martin, and J. Beckwith. 1996. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. USA 93:13048-13053.
32. Russel, M. 1995. Thioredoxin genetics. Methods Enzymol. 252:264-274.
33. Russel, M., and P. Model. 1986. The role of thioredoxin in filamentous phage assembly. J. Biol. Chem. 261:14997-15005.
34. Sambongi, Y., and S. J. Ferguson. 1994. Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein. FEBS Lett. 353:235-238.
35. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, (2nd ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
36. Saxena, V. P., and D. B. Wetlaufer. 1970. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9:5015-5022.
37. Shevchik, V. E., G. Condemine, and B. J. Robert. 1994. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13:2007-2012.
38. Sone, M., Y. Akiyama, and K. Ito. 1997. Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds. J. Biol. Chem. 272:10349-10352.
39. 38a.Stewart, E. Unpublished data.
40. Walker, K. W., and H. F. Gilbert. 1997. Scanning and escape during protein-disulfide isomerase assisted protein folding. J. Biol. Chem. 272:8845-8848.
41. Walker, K. W., M. M. Lyles, and H. F. Gilbert. 1996. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35:1972-1980.
42. Wunderlich, M., A. Otto, K. Maskos, M. Mucke, R. Seckler, and R. Glockshuber. 1995. Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol. 247:28-33.
43. Zapun, A., D. Missiakas, S. Raina, and T. E. Creighton. 1995. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34:5075-5089.