Aggregation as the basis for complex behaviour of cutinase in different denaturants

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 2, 2007, Pages 323-333

  Otzen, Daniel E ^a   Giehm, Lise ^a   Baptista, Ricardo P ^c   Kristensen, Søren R ^b   Melo, Eduardo P ^c,d   Pedersen, Shona ^a,b  

^a AALBORG UNIVERSITY   (Denmark)

^b AALBORG UNIVERSITY HOSPITAL   (Denmark)

^c INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^d UNIVERSITY OF ALGARVE   (Portugal)

Author keywords

Aggregation; Cutinase; Denaturant; Folding scheme; Guanidinium thiocyanate

Indexed keywords

CUTINASE; GUANIDINE; GUANIDINE THIOCYANATE; THIOCYANIC ACID DERIVATIVE; UNCLASSIFIED DRUG; UREA;

ARTICLE; ENZYME DENATURATION; EQUILIBRIUM CONSTANT; HYDROPHOBICITY; KINETICS; PH; PRIORITY JOURNAL;

CARBOXYLIC ESTER HYDROLASES; GUANIDINE; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 33846795794     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.11.012     Document Type: Article

References (47)

1. Tanford C. Protein denaturation: Part A. Characterization of the denatured state. Adv. Protein Chem. 23 (1968) 121-217
2. Tanford C. Protein denaturation: Part B. The transition from native to denatured state. Adv. Protein Chem. 23 (1968) 218-282
3. Tanford C. Protein denaturation. Part C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24 (1970) 1-95
4. Baldwin R. On-pathway versus off-pathway folding intermediates. Fold. Des. 1 (1996) R1-R8
5. Baldwin R.L. How Hofmeister ion interactions affect protein stability. Biophys. J. 71 (1996) 2056-2063
6. Fersht A.R. Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding (1999), Freeman & Co., New York
7. Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-279
8. Morjana N.A., McKeone B.J., and Gilbert H.F. Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 2107-2111
9. Boren K., Grankvist H., Hammarstrom P., and Carlsson U. Reshaping the folding energy landscape by chloride salt: impact on molten-globule formation and aggregation behavior of carbonic anhydrase. FEBS Lett. 566 (2004) 95-99
10. Otzen D.E., and Fersht A.R. Folding of circular and permuted Chymotrypsin Inhibitor 2: retention of the folding nucleus. Biochemistry 37 (1998) 8139-8146
11. Perez-Jimenez R., Godoy-Ruiz R., Ibarra-Molero B., and Sanchez-Ruiz J.M. The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect?. Biophys. J. 86 (2004) 2414-2429
12. Zeeb M., Lipps G., Lilie H., and Balbach J. Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus. J. Mol. Biol. 336 (2004) 227.240
13. Sanz J.M., and Fersht A.R. Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. Biochemistry 32 (1993) 13584-13592
14. Matouschek A., Kellis J.T., Serrano L., Bycroft M., and Fersht A.R. Transient folding intermediates characterized by protein engineering. Nature 346 (1990) 440-445
15. Otzen D.E., and Oliveberg M. Salt-induced detour through compact regions of the protein folding landscape. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 11746-11751
16. Sosnick T.R., Mayne L., and Englander S.W. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins 24 (1996) 413-426
17. Krantz B.A., Mayne L., Rumbley J., Englander S.W., and Sosnick T.R. Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. J. Mol. Biol. 324 (2002) 359-371
18. Eaton W.A., Thompson P.A., Chan C.K., Hagen S.J., and Hofrichter J. Fast events in protein folding. Structure 4 (1996) 1133-1139
19. Longhi S., and Cambillau C. Structure-activity of cutinase, a small lipolytic enzyme. Biochim. Biophys. Acta 1441 (1999) 185-196
20. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J., et al. The alpha/beta hydrolase fold. Protein Eng. 5 (1992) 197-211
21. Melo E.P., Faria T.Q., Martins L.O., Goncalves A.M., and Cabral J.M. Cutinase unfolding and stabilization by trehalose and mannosylglycerate. Proteins 42 (2001) 542-552
22. Melo E.P., Chen L., Cabral J.M., Fojan P., Petersen S.B., and Otzen D.E. Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry 42 (2003) 7611-7617
23. Poulsen K.R., Sørensen T.K., Duroux L., Petersen E.I., Petersen S.B., and Wimmer R. The interaction of Fusarium solani pisi cutinase with long chain spin label esters. Biochemistry 45 (2006) 9163-9171
24. Pedersen S., Nesgaard L.W., Baptista R.P., Melo E.P., Kristensen S.R., and Otzen D.E. pH-dependent aggregation of cutinase is efficiently suppressed by 1,8-ANS. Biopolymers 83 (2006) 619-629
25. Clarke J., and Fersht A.R. Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry 32 (1993) 4322-4329
26. Melo E.P., Chen L., Cabral J.M., Fojan P., Petersen S.B., and Otzen D.E. Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry 42 (2003) 7611-7617
27. Otzen D.E., Kristensen O., Proctor M., and Oliveberg O. Structural changes in the transition state of protein folding: an alternative interpretation of curved chevron plots. Biochemistry 38 (1999) 6499-6511
28. Melo E.P., Faria T.Q., Martins L.O., Goncalves A.M., and Cabral J.M. Cutinase unfolding and stabilization by trehalose and mannosylglycerate. Proteins: Struct. Funct. Genet. 42 (2001) 542-552
29. Jackson S.E., and Fersht A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30 (1991) 10428-10435
30. Silow M., and Oliveberg M. High-energy channelling in protein folding. Biochemistry 36 (1997) 7633-7637
31. Otzen D.E. Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis. Prot. Eng. Des. Sel. 18 (2005) 547-557
32. Goldstein R.F., and Stryer L. Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy. Biophys. J. 50 (1986) 583-599
33. Timasheff S. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 41 (2002) 13473-13482
34. Mogensen J.E., Ibsen H., Lund J., and Otzen D.E. Elimination of an off-pathway folding intermediate by a single point mutation. Biochemistry 43 (2004) 3357-3367
35. Parker M.J., Spencer J., and Clarke A.R. An Integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253 (1995) 771-786
36. Parker M.J., Dempsey C.E., Lorch M., and Clarke A.R. Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. Biochemistry 36 (1997) 13396-13405
37. Nozaki Y., and Tanford C. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions. J. Biol. Chem. 245 (1970) 1648-1652
38. Creighton T.E. Electrophoretic analysis of the unfolding of proteins by urea. J. Mol. Biol. 129 (1979) 235-264
39. von Hippel P.H., and Wong K.Y. On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J. Biol. Chem. 240 (1965) 3909-3923
40. Dill K.A., and Shortle D. Denatured states of proteins. Ann. Rev. Biochem. 60 (1991) 795-825
41. Shi Z., Chen K., Liu Z., and Kallenbach N.R. Conformation of the backbone in unfolded proteins. Chem. Rev. 106 (2006) 1877-1897
42. Chen L.Y., Cabrita G.J.M., Otzen D.E., and Pinho e Melo E. Stabilization of the ribosomal protein S6 by trehalose is counterbalanced by the formation of a putative off-pathway species. J. Mol. Biol. 351 (2005) 402-416
43. Otzen D.E., Kristensen P., and Oliveberg M. Designed protein tetramer zipped together with an Alzheimer sequence: a structural clue to amyloid assembly. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 9907-9912
44. Gitlin I., Gudiksen K.L., and Whitesides G.M. Effects of surface charge on denaturation of bovine carbonic anhydrase. ChemBioChem 7 (2006) 1241-1250
45. J.S. Pedersen, D. Dikov, D.E. Otzen, N- and C-terminal hydrophobic patches are involved in fibrillation of glucagon, Biochemistry 45 (2006) 14503-14512.
46. Pedersen J.S., Dikov D., Flink J.L., and Otzen D.E. Sulfates dramatically stabilize a salt dependent type of glucagon fibrils. Biophys. J. 90 (2006) 4181-4194
47. Pedersen J.S., Dikov D., Flink J.L., Hjuler H.A., Christiansen G., and Otzen D.E. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J. Mol. Biol. 355 (2006) 501-523