Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases

Protein Science

Volumn 7, Issue 5, 1998, Pages 1233-1244

  Mössner, Ekkehard ^a   Huber Wunderlich, Martina ^a   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

Author keywords

Cys Xaa Xaa Cys motif; DsbA; Glutaredoxin; pK(a) values; Protein disulfide isomerase; Protein stability; Redox potentials; Thioredoxin

Indexed keywords

CYSTEINE; DIPEPTIDE; DISULFIDE; ENZYME VARIANT; GLUTATHIONE; IODOACETAMIDE; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; THIOL DERIVATIVE; THIOREDOXIN;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; EQUILIBRIUM CONSTANT; ESCHERICHIA COLI; MOLECULAR MIMICRY; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PKA; PRIORITY JOURNAL; PROTEIN STABILITY; SEQUENCE HOMOLOGY; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0039714219     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070519     Document Type: Article

References (57)

1. Åslund F. 1996. Glutaredoxins [Thesis]. Stockholm: Karolinska Institutet Stockholm.
2. Bachmann BJ. 1972. Pedigrees of some mutant strains of Escherichia coli K12. Bacteriol Rev 36:525-557.
3. Bushweller JH, Åslund F, Wüthrich K, Holmgren A. 1992. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14S) and its mixed disulfide with glutathione. Biochemistry 31:9288-9293.
4. Chivers PT, Lahoissiere MCA, Raines RT. 1996. The CXXC motif: Imperatives for the formation of native disulfide bonds in the cell. EMBO J 15:2659-2667.
5. Chivers PT, Prehoda KE, Raines RT. 1997. The CXXC motif: A rheostat in the active site. Biochemistry 36:4061-4066.
6. Darby NJ, Creighton TE. 1995. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34:16770-16780.
7. Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS, Kuprin S, Holmgren A. 1997. Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: Structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 36:2622-2636.
8. Ellman GL. 1959. Tissue sulfhydryl groups. Arch Biochem Biophys 82:70-77.
9. Forman-Kay JD, Clore GM, Gronenborn AM. 1992. Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo-and heteronuclear NMR. Biochemistry 31:3442-3452.
10. Freedman RB, Hirst TR, Tuite MF. 1994. Protein disulphide isomerase: Building bridges in protein folding. Trends Biochem Sci 19:331-336.
11. Gan ZR, Sardana MK, Jacobs JW, Polokoff MA. 1990. Yeast thioltransferase: The active-site cysteines display differential reactivity. Arch Biochem Biophys 252:110-115.
12. Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Analyt Biochem 182:319-326.
13. Grauschopf U, Winther JR, Korber P, Zander TP, Dallinger P, Bardwell JCA. 1995. Why is DsbA such an oxidizing disulfide catalyst? Cell 83:947-955.
14. Guddat LW, Bardwell JCA, Zander T, Martin JL. 1997a. The uncharged surface features surrounding the active site of Escherichia coli DshA are conserved and are implicated in peptide binding. Protein Sci 6:1148-1156.
15. Guddat LW, Bardwell JCA, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL. 1997b. Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His 32 in DshA stability. Protein Sci 6:1893-1900.
16. Hol WGJ. 1985. The role of the α-helix dipole in protein function and structure. Prog Biophys Molec Biol 45:149-195.
17. Holmgren A. 1972. Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin. J Biol Chem 247:1992-1998.
18. Holmgren A. 1995. Thioredoxins and glutaredoxins. In: Packer L, ed. Methods in enzymology, biothiols: Part B. New York: Academic Press. pp 199-209.
19. Holst B, Tachibana C, Winther JR. 1997. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138:1229-1238.
20. Huber-Wunderlich M, Glockshuber R. 1998. Folding and design 3:161-171.
21. Jacobi A, Huber-Wunderlich M, Hennecke J, Glockshuber R. 1997. Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. J Biol Chem 272:21692-21699.
22. Jeng MF, Campbell AP, Begley T, Holmgren A, Case DA, Wright PE, Dyson HJ. 1994. High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2:853-868.
23. Jeng MF, Holmgren A, Dyson HJ. 1995. Proton sharing between cysteine thiols in Escherichia coli thioredoxin: Implications for the mechanism of protein disulfide reduction. Biochemistry 34:10101-10105.
24. Kallis GB, Holmgren A. 1980. Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J Biol Chem 255:10261-10265.
25. Katti SK, LeMaster DM, Eklund H. 1990. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212:167-184.
26. Katti SK, Robbins AH, Yang Y, Wells WW. 1995. Crystal structure of thioltransfersae at 2.2 Å resolution. Protein Sci 4:1998-2005.
27. a values in proteins of the thioredoxin family. J Mol Biol 253:799-812.
28. Kortemme T, Darby NJ, Creighton TE. 1996. Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Biochemistry 35:14503-14511.
29. Krause G, Lundström J, Barea JL, Pueyo de la Cuesta C, Holmgren A. 1991. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Escherichia coli thioredoxin. J Biol Chem 266:9494-9500.
30. Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154:362-382.
31. a values of active-center cysteines, cysteines-32 and -35, in Escherichia coli thioredoxin by Raman spectroscopy. Biochemists 32:5800-5808.
32. Lin T-Y, Kim PS. 1989. Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry 28:5282-5287.
33. Loferer H, Wunderlich M, Hennecke H, Glockshuber R. 1995. A bacterial thioredoxin-like protein that is exposed to the periplasm has redox properties comparable with those of cytoplasmic thioredoxins. J Biol Chem 270: 26178-26183.
34. Lundström J, Holmgren A. 1993. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32:6649-6655.
35. Martin JL. 1995. Thioredoxin - A fold for all reasons. Structure 3:245-250.
36. Nelson JW, Creighton TE. 1994. Reactivity and ionization of the active site cysteine residues of DshA, a protein required for disulfide bond formation in vivo. Biochemistry 33:5974-5983.
37. Pace CN. 1986. Determination and analysis urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
38. Qin J, Clore GM, Gronenborn AM. 1994. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2:503-522.
39. Rossmann R, Stern D, Loferer H, Jacobi A, Glockshuher R, Hennecke H. 1997. Replacement of Pro109 by His in TlpA, a thioredoxin-like protein from Bradyrhyzobium japonicum, alters its redox properties but not its in vivo functions. FEBS Lett 406:249-254.
40. Rost J, Rapoport S. 1964. Reduction-potential of glutathione. Nature 201:185.
41. Ruddock LW, Hirst TR, Freedman RB. 1996. pH dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide isomerase: Studies with a novel simple peptide substrate. Biochem J 315:1001-1005.
42. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: A laboratory manual. New York: Cold Spring Harbor.
43. Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
44. Strobl S, Mühlhahn P, Bernstein R, Witscheck R, Maskos K, Wunderlich M, Huber R, Glockshuber R, Holak TA. 1995. Determination of the three dimensional structure of the bifunctional α-amylase/trypsin inhibitor from Ragi seeds by NMR spectroscopy. Biochemistry 34:8281-8293.
45. Studier FW, Moffat BA. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130.
46. Szajewski RP, While-sides GM. 1980. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione. J Am Chem Soc 102:2011-2026.
47. Takahashi N, Creighton TE. 1996. On the reactivity and ionization of the active site cysteine residues of Escherichia coli thioredoxin. Biochemistry 35:8342-8353.
48. Weichsel A, Gasdaska JR, Powis G, Montfort WR. 1996. Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer. Structure 4:735-751.
49. Weissman JS, Kim PS. 1993. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365:185-188.
50. Wunderlich M, Glockshuber R. 1993. Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci 2:717-726.
51. Wunderlich M, Otto A, Seckler R, Glockshuber R. 1993. Bacterial protein disulfide isomerase: Efficient catalysis of oxidative protein folding at acidic pH. Biochemistry 32:12251-12256.
52. Wunderlich M, Otto A, Maskos K, Mücke M, Seckler R, Glockshuber R. 1995. Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J Mol Biol 247:28-33.
53. Xia TH, Bushweller JH, Sodano P, Billeter M, Bjornberg O, Holmgren A, Wüthrich K. 1992. NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Sci 1:310-321.
54. Yang Y, Wells WW. 1991. Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site directed mutagenesis. J Biol Chem 19:12759-12765.
55. Zapun A, Bardwell JC, Creighton TE. 1993. The reactive and destabilizing disulfide bond of DshA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32:5083-5092.
56. Zapun A, Cooper L, Creighton TE. 1994. Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33:1907-1914.
57. Zapun A, Missiakas D, Raina S, Creighton TE. 1995. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemists 34:5075-5089.