The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency

Journal of Molecular Biology

Volumn 276, Issue 1, 1998, Pages 239-247

  Darby, Nigel J ^a   Penka, Elke ^a   Vincentelli, Renaud ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Duslufide bond; PDI; Protein folding; Thioredoxin

Indexed keywords

DISULFIDE; PROTEIN DISULFIDE ISOMERASE; THIOL;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; MUTAGENESIS; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING;

EID: 0032512878     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1504     Document Type: Article

References (45)

1. Chaudhuri M.M., Tonin P.N., Lewis W.H., Srinivasan P.R. The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phopholipase C family, is amplified in hydroxyurea-resistant cells. Biochem. J. 281:1992;645-650
2. Creighton T.E., Bagley C.J., Cooper L., Darby N.J., Freedman R.B., Kemmink J., Sheikh A. On the biosynthesis of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 232:1993;1176-1196
3. Creighton T.E., Zapun A., Darby N.J. Mechanisms and catalysis of disulphide bond formation in proteins. Trends. Biotechnol. 13:1995;18-22
4. Creighton T.E., Darby N.J., Kemmink J. The roles of partly folded intermediates in protein folding. FASEB. J. 10:1996;100-118
5. Darby N.J., Creighton T.E. Functional properties of the thioredoxin-like domains of protein disulphide isomerase. Biochemistry. 34:1995;11725-11735
6. Darby N.J., Creighton T.E. Characterisation of the active site cysteine residues of protein disulphide isomerase. Biochemistry. 43:1995;16770-16780
7. Darby N.J., Creighton T.E. The catalytic mechanism of DsbA comparison with protein disulphide isomerase. Biochemistry. 34:1995;3576-3587
8. Darby N.J., Freedman R.B., Creighton T.E. Dissecting the mechanism of disulphide bond formation by protein disulphide isomerase. Biochemistry. 33:1994;7937-7947
9. Darby N.J., Morin P.E., Talbo G., Creighton T.E. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide bonds. J. Mol. Biol. 249:1995;463-477
10. Darby N.J., Kemmink J., Creighton T.E. Identification of a non-catalytic domain of protein disulphide isomerase. Biochemistry. 35:1996;10517-10528
11. Darby N.J., Creighton T.E. Disulphide bonds in protein folding and stability. Methods Mol. Biol. 40:1996;219-253
12. Darby N.J., Raina S., Creighton T.E. The role of substrate binding in the catalytic mechanism of DsbC. Biochemistry. 1998;. In the press
13. Edman J.C., Ellis L., Blacher R.W., Roth R.A., Rutter W.J. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature. 317:1985;267-270
14. Freedman R.B., Hirst T.R., Tuite M.F. Protein disulphide isomerase building bridges in protein folding. Trends. Biochem. Sci. 19:1994;331-336
15. Gaudet R., Bohm A., Sigler P.B. Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosphoducin. Cell. 87:1996;577-588
16. Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326
17. Givol D., DeLorenzo F., Goldberger R.F., Anfinsen C.B. Disulphide interchange and the three dimensional structure of proteins. Proc. Natl Acad. Sci. USA. 53:1965;676-684
18. Gordon D.A., Wetterau J.R., Gregg R.E. Microsomal triglyceride transfer protein; a protein complex required for the assembly of lipoprotein particles. Trends. Cell Biol. 5:1995;317-321
19. Hawkins H.C., Freedman R.B. The reactivities and ionization properties of the active site dithiol groups of mammalian protein disulphide isomerase. Biochem. J. 275:1991;335-339
20. Hayano T., Hirose M., Kikuchi M. Protein disulphide isomerase lacking its isomerase activity accelerates folding in the cell. FEBS Letters. 377:1995;505-511
21. Holmgren A. Thioredoxin structure and mechanism; conformational changes on oxidation of the active site sulphydryls to a disulphide. Structure. 3:1995;239-243
22. Kallis G.-B., Holmgren A. Differential reactivity of the functional sulphydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 255:1980;10261-10265
23. 15NMR spectroscopy. Biochemistry. 35:1996;7684-7691
24. Kemmink J., Darby N.J., Dijstra K., Nilges M., Creighton T.E. The folding catalyst protein disulphide isomerase is constructed of active and inactive thioredoxin modules. Curr. Biol. 7:1997;239-245
25. Klappa P., Hawkins H.C., Freedman R.B. Interactions between protein disulphide isomerase and peptides. Eur. J. Biochem. 248:1997;37-42
26. Kortemme T., Darby N.J., Creighton T.E. Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulphide isomerase. Biochemistry. 35:1996;14503-14511
27. Lamberg A., Juahiainen M., Metso J., Ehnholm C., Shoulders C., Scott J., Pihlajaniemi T., Kivirriko K.I. The role of protein disulphide isomerase in the microsomal triacylglycerol transfer protein does not reside in its isomerase activity. Biochem. J. 315:1996;533-536
28. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 27:1970;680-685
29. Lunström J., Holmgren A. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulphide isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry. 32:1993;6649-6655
30. Lyles M.M., Gilbert H.F. Mutations in the thioredoxin sites of protein disulphide isomerase reveal functional non-equivalence of N and C-terminal domains. J. Biol. Chem. 269:1994;30946-30952
31. Martin J. Thioredoxin- a fold for all reasons. Structure. 3:1995;245-250
32. Mazzarella R.A., Srinivasan M., Haugejorden S.M., Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulphide isomerase. J. Biol. Chem. 265:1990;1094-1101
33. Morjana N.A., Gilbert H.F. Effect of protein and peptide inhibitors on the activity of protein disulphide isomerase. Biochemistry. 30:1991;4985-4990
34. Noiva R., Freedman R.B., Lennarz W.J. Peptide binding to protein disulphide isomerase occurs at a site distinct from the active sites. J. Biol. Chem. 268:1993;19210-19217
35. Pihlajaniemi T., Helaakoski T., Tasanen K., Myllyla R., Huhtala M.-L., Koivu J., Kivirriko K.I. Molecular cloning of the β-subunit of prolyl-4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6:1987;643-649
36. Puig A., Gilbert H.F. Protein disulphide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 269:1994;7764-7771
37. Sarkar G., Sommer S.S. The "megaprimer" method of site directed mutagenesis. BioTechniques. 8:1990;289-297
38. Studier F.W., Rosenberg A.H., Dunn J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:1990;60-89
39. Tachikawa H., Takeuchi Y., Funahashi W., Miura T., Goa X.D., Fujimoto D., Mizunaga T., Onodera K. Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulphide isomerase depletion. FEBS Letters. 369:1995;212-216
40. Veijola J., Pihlajaniemi T., Kivirriko K.I. Co-expression of the α subunit of human prolyl-4-hydroxylase with BiP polypeptide in insect cells leads to the formation of soluble and insoluble complexes. Biochem. J. 315:1996;613-618
41. Vuori K., Myllylä R., Pihlajaniemi T., Kivirikko K.I. Expression and site directed mutagenesis of human protein disulphide isomerase in Escherichia coli. J. Biol. Chem. 267:1992;7211-7214
42. Walker K.W., Gilbert H.F. Oxidation of kinetically trapped thiols by protein disulphide isomerase. Biochemistry. 34:1995;13642-13650
43. 2. EMBO J. 16:1997;651-658
44. Zapun A., Creighton T.E. Effects of DsbA on the disulphide folding of bovine pancreatic trypsin inhibitor and α-lactalbumin. Biochemistry. 33:1994;5202-5211
45. Zapun A., Missiakas D., Raina S., Creighton T.E. Structure and functional characterization of DsbC, a protein involved in disulphide bond formation in Escherichia coli. Biochemistry. 34:1995;5075-5089