Preferential binding of an unfolded protein to DsbA

EMBO Journal

Volumn 15, Issue 2, 1996, Pages 392-398

  Frech, Christian ^a   Wunderlich, Martina ^b   Glockshuber, Rudi ^b   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b ETH ZURICH   (Switzerland)

Author keywords

Disulfide bonds; Folding catalysis; Folding intermediates; Protein folding; Protein stability

Indexed keywords

BACTERIAL ENZYME; OXIDOREDUCTASE; RIBONUCLEASE T1;

ARTICLE; BINDING SITE; DISULFIDE BOND; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030028838     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00369.x     Document Type: Article

References (40)

1. Bardwell, J.C.A. and Beckwith, J. (1993) The bonds that tie - catalyzed disulfide bond formation. Cell, 74, 769-771.
2. Bardwell, J.C.A., McGovern, K. and Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell, 67, 581-590.
3. Bardwell, J.C.A , Lee, J.-O., Jander, G., Martin, N , Belin, D. and Beckwith, J. (1993) A pathway for disulfide formation in vivo. Proc. Natl Acad. Sci. USA, 90, 1038-1042.
4. Bulleid, N.J. and Freedman, R.B. (1988) Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature, 335, 649-651.
5. Cai, H., Wang, C.C. and Tsou, C.L. (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds J. Biol. Chem., 269, 24550-24552.
6. Creighton, T.E. (1986) Disulfide bonds as probes of protein folding pathways. Methods Enzymol., 131, 83-106.
7. Creighton, T.E. (1992) Folding pathways determined using disulfide bonds. In Creighton, T.E. (ed.), Prorein Folding. W.H. Freeman, New York, pp. 301-351.
8. Darby, N.J. and Creighton, T.E. (1993) Dissecting the disulfide-coupled folding pathway of bovine pancreatic trypsin inhibitor. J. Mol Biol., 232, 873-896.
9. Darby, N J. and Creighton, T.E. (1995) Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry, 34, 3576-3587.
10. Darby, N.J., Freedman, R.B. and Creighton, T E. (1994) Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide. Biochemistry, 33, 7937-7947.
11. Fischer, G., Bang, H. and Mech, C. (1984) Nachweis einer Enzymkatalyse für die cis-trans-Isomerisierung der Peptidbindung in prolinhaltigen Peptiden. Biomed. Biochim. Acta, 43, 1101-1111
12. Frech, C. and Schmid, F.X (1995) Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1. J. Mol Biol., 251, 135-149.
13. Freedman, R.B., Hirst, T.R. and Tuite, M.F. (1994) Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci., 19, 331-336.
14. Goldenberg, D.P. (1992) Native and non-native intermediates in the BPTI folding pathway. Trends Biochem. Sci., 17, 257-261.
15. Laminet, A.A. and Plückthun, A (1989) The precursor of beta-lactamase: purification, properties and folding kinetics. EMBO J., 8, 1469-1477.
16. Martin, J L., Bardwell, J.C A. and Kuriyan, J. (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature, 365, 464-468.
17. Mayr, L M. and Schmid, F.X. (1993) A purification method for labile variants of ribonuclease T1. Protein Expr. Purif., 4, 52-58.
18. Mayr, L.M., Willbold, D., Landt, O. and Schmid, F.X. (1994) Role of the Cys2-Cys10 disulfide bond for the stability and folding kinetics of ribonuclease T1 Protein Sci., 3, 227-239.
19. Mücke, M. and Schmid, F.X. (1992) Enzymatic catalysis of prolyl isomerization in an unfolding protein. Biochemistry, 31, 7848-7854.
20. Mücke, M and Schmid, F.X. (1994a) Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds. Biochemistry, 33, 14608-14619.
21. Mücke, M. and Schmid, F.X. (1994b) Intact disulfide bonds decelerate the folding of ribonuclease T1. J. Mol Biol., 239, 713-725
22. Mücke, M. and Schmid, F.X. (1994c) A kinetic method to evaluate the two-state character of solvent-induced protein denaturation. Biochemistry, 33, 12930-12935.
23. Nelson, J.W and Creighton, T.E. (1994) Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry, 33, 5974-5983.
24. Pace, C.N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol., 131, 266-280.
25. Pace, C.N , Grimsley, G.R., Thomson, J.A. and Barnett, B.J (1988) Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem., 263, 11820-11825.
26. Quaas, R., Grunert, H.-P., Kimura, M and Hahn, U. (1988) Expression of ribonuclease T1 in Escherichia coli and rapid purification of the enzyme. Nucleosides and Nucleotides, 7, 619-623.
27. Riddles, P.W., Blakely, R.L. and Zerner, B. (1983) Reassessment of Ellman's reagent. Methods Enzymol., 49, 49-60.
28. Ruoppolo, M. and Freedman, R.B. (1994) Protein-S-S-glutathione mixed disulfides as models of unfolded proteins. Biochemistry, 33, 7654-7662
29. Santoro, M.M. and Bolen, D W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry, 27, 8063-8068.
30. Takahashi, K., Uchida, T and Egami, F. (1970) Ribonuclease T1: structure and function. Adv Biophys., 1, 53-98.
31. Tanford, C. (1968) Protein denaturation. Part B. The transition state from native to denatured state. Adv. Protein Chem., 23, 218-282.
32. Walker, K.W. and Gilbert, H.F. (1994) Effect of redox environment on the in vitro and in vivo folding of RTEM-1 beta-lactamase and Escherichia coli alkaline phosphatase. J. Biol. Chem., 269, 28487-28493.
33. Weissman, J.S. and Kim, P S. (1991) Reexamination of the folding of BPTI. predominance of native intermediates. Science, 253, 1386-1393.
34. Wunderlich, M. and Glockshuber, R (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci., 2, 717-726.
35. Wunderlich, M., Jaenicke, R. and Glockshuber, R (1993a) The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form. J. Mol Biol., 233, 559-566.
36. Wunderlich, M., Otto, A., Seckler, R. and Glockshuber, R. (1993b) Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH. Biochemistry, 32, 12251-12256.
37. Wunderlich, M., Otto, A., Maskos, K., Mucke, M., Seckler, R. and Glockshuber, R. (1995) Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol., 247, 28-33.
38. Zapun, A., Creighton, T.E., Rowling, P.J.E. and Freedman, R.B. (1992) Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum. Protein Struct. Funct Genet , 14, 10-15.
39. Zapun, A., Bardwell, J.C.A. and Creighton, T E. (1993) The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry, 32, 5083-5092
40. Zapun, A., Cooper, L. and Creighton, T.E. (1994) Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry, 33, 1907-1914