Non-redox-active small-molecules can accelerate oxidative protein folding by novel mechanisms

Biophysical Chemistry

Volumn 132, Issue 2-3, 2008, Pages 104-109

  Fink, Matthew ^a   Nieves, Paul ^b   Chang, Saemin ^a   Narayan, Mahesh ^a  

^a UNIVERSITY OF TEXAS AT EL PASO   (United States)

^b Universidad Metropolitana   (Puerto Rico)

Author keywords

(+ ) trans 1,2 bis(2 mercaptoacetamido)cyclohexane; 2 aminoethanethiosulfonate; AEMTS; BMC; dithiothreitol; DTT; high performance liquid chromatography; HPLC; Native tendency; Oxidative folding; Small molecule; Thiol disulfide exchange

Indexed keywords

1,2 BIS(2 MERCAPTOACETAMIDO)CYCLOHEXANE; CYSTEINE; DISULFIDE; RIBONUCLEASE A; THIOL; TRIFLUOROETHANOL; TRIMETHYLAMINE OXIDE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATION; DISULFIDE BOND; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE;

ANIMALS; CATTLE; DISULFIDES; ENZYME STABILITY; KINETICS; ORGANIC CHEMICALS; OXIDATION-REDUCTION; PROTEIN FOLDING; RIBONUCLEASE, PANCREATIC;

BOVINAE;

EID: 37049015084     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.10.014     Document Type: Article

References (33)

1. Narayan M., Welker E., Wedemeyer W.J., and Scheraga H.A. Oxidative folding of proteins. Acc. Chem. Res. 33 (2000) 737-820
2. Woycechowsky K.J., and Raines R.T. Native disulfide bond formation in proteins. Curr. Opin. Chem. Biol. 4 (2000) 533-539
3. Arolas J.L., Aviles F.X., Chang J.Y., and Ventura S. Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem. Sci. 31 (2006) 292-301
4. Tu B.P., and Weissman J.S. Oxidative protein folding in eukaryotes: mechanisms and consequences. J. Cell Biol. 164 (2004) 341-346
5. Wedemeyer W.J., Welker E., Narayan M., and Scheraga H.A. Disulfide bonds and protein folding. Biochemistry 39 (2000) 4207-4216
6. Welker E., Narayan M., Wedemeyer W.J., and Scheraga H.A. Structural determinants of oxidative folding in proteins. PNAS USA 98 (2001) 2312-2316
7. Welker E., Wedemeyer W.J., Narayan M., and Scheraga H.A. Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins. Biochemistry 40 (2001) 9059-9064
8. Rothwarf D.M., and Scheraga H.A. Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution. Biochemistry 32 (1993) 2671-2679
9. Rothwarf D.M., Li Y.J., and Scheraga H.A. Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways. Biochemistry 37 (1998) 3760-3766
10. Iwaoka M., Wedemeyer W.J., and Scheraga H.A. Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactions. Biochemistry 38 (1999) 2805-2815
11. Xu X., Rothwarf D.M., and Scheraga H.A. Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A. Biochemistry 35 (1996) 6406-6417
12. Volles M.J., Xu X., and Scheraga H.A. Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: further insights into the folding process. Biochemistry 38 (1999) 7284-7293
13. Hawkins H.C., and 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
14. Weissman J.S., and Kim P.S. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365 (1993) 185-188
15. Wilkinson B., and Gilbert H.F. Protein disulfide isomerase. Biochim. Biophys. Acta 1699 (2004) 35-44
16. Tian G., Xiang S., Noiva R., Lennarz W.J., and Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124 (2006) 61-73 (Erratum in: Cell 124 (2006) 1085-1088)
17. Shin H.C., and Scheraga H.A. Catalysis of the oxidative folding of bovine pancreatic ribonuclease A by protein disulfide isomerase. J. Mol. Biol. 300 (2004) 995-1003
18. Mattson M.P. Nitro-PDI incites toxic waste accumulation. Nat. Neurosci. 9 (2006) 865-867
19. Uehara T., Nakamura T., Yao D., Shi Z.Q., Gu Z., Ma Y., Masliah E., Nomura Y.S., and Lipton S.A. S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 441 (2006) 513-517
20. Kersteen E.A., and Raines R.T. R.T. Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics. Antioxid. Redox Signal. 5 (2003) 413-424
21. Chivers P.T., Laboissiere M.C., and Raines R.T. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 15 (1996) 2659-2667
22. Xu G., Narayan M., and Scheraga H.A. The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide. Biochemistry 44 (2005) 9817-9823
23. Shi T., and Rabenstein D.L. trans-Dichlorotetracyanoplatinate (IV) as a reagent for the rapid and quantitative formation of intramolecular disulfide bonds in peptides. J. Org. Chem. 64 (1999) 4590-4595
24. Narayan M., Welker E., and Scheraga H.A. Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins. J. Am. Chem. Soc. 123 (2003) 2909-2910
25. Gilbert H.F. Protein disulfide isomerase. Methods Enzymol. 290 (1998) 26-50
26. Fewell S.W., Travers K.J., Weissman J.S., and Brodsky J.L. The action of molecular chaperones in the early secretory pathway. Annu. Rev. Genet. 35 (2001) 149-191
27. Gough J.D., Barrett E.J., Silva Y., and Lees W.J. ortho- and meta-substituted aromatic thiols are efficient redox buffers that increase the folding rate of a disulfide-containing protein. J. Biotechnol. 125 (2006) 39-47
28. Saito K., Welker E., and Scheraga H.A. Folding of a disulfide-bonded protein species with free thiol(s): competition between conformational folding and disulfide reshuffling in an intermediate of bovine pancreatic ribonuclease A. Biochemistry 40 (2001) 15002-15008
29. Baskakov I., and Bolen D.W. Forcing thermodynamically unfolded proteins to fold. J. Biol. Chem. 273 (1998) 4831-4834
30. Bolen D.W. Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization. Methods 34 (2004) 312-322
31. Buck M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31 (1998) 297-355
32. Shiraki K., Nishikawa K., and Goto Y. Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245 2 (Jan 13 1995) 180-194
33. Romisch K. A cure for traffic jams: small molecule chaperones in the endoplasmic reticulum. Traffic 5 (2004) 815-820