Elongation in a β-structure promotes amyloid-like fibril formation of human lysozyme

Journal of Biochemistry

Volumn 132, Issue 4, 2002, Pages 655-661

  Goda, Shuichiro ^a   Takano, Kazufumi ^a   Yamagata, Yuriko ^b   Maki, Saori ^c   Namba, Keiichi ^a,c,d   Yutani, Katsuhide ^a,e  

^a OSAKA UNIVERSITY   (Japan)

^b KUMAMOTO UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d PANASONIC CORPORATION   (Japan)

^e KWANSEI GAKUIN UNIVERSITY   (Japan)

Author keywords

Amyloid formation; Amyloidogenicity; Conformational stability; Mutant human lysozyme

Indexed keywords

ALCOHOL; AMYLOID; LYSOZYME; AMYLOID PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON MICROSCOPY; ENZYME STABILITY; GENETICS; HUMAN; KINETICS; METHODOLOGY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS; ULTRASTRUCTURE; X RAY DIFFRACTION; ALPHA HELIX; AMINO TERMINAL SEQUENCE; BETA CHAIN; CONFORMATIONAL TRANSITION; FIBER; MOLECULAR STABILITY; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

AMINO ACID SUBSTITUTION; AMYLOID; ENZYME STABILITY; ETHANOL; HUMANS; KINETICS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MURAMIDASE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; X-RAY DIFFRACTION;

EID: 0036775896     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003270     Document Type: Article

References (42)

1. Dobson, C.M. (1999) Protein misfolding, evolution and disease. Trends. Biochem. Sci. 24, 329-332
2. Tan, S.Y. and Pepys, M.B. (1994) Amyloidosis. Histopathology 25, 403-414
3. Kelly, J.W. (1996) Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6, 11-17
4. Perutz, M.F. (1999) Glutamine repeats and neurodegenerative disease molecular aspects. Trends. Biochem. Sci. 24, 58-63
5. Rochet, J.-C. and Lansbury, Jr.P.T. (2000) Amyloid fibrillogenesis: Themes and variations. Curr. Opin. Struct. Biol. 10, 60-68
6. Wall, J., Schell, M., Murphy, C., Hrncic, R., Stevens, F.J., and Solomon, A. (1999) Thermodynamic instability of human λ6 light chains: Correction with fibrillogenecity. Biochemistry 38, 14101-14108
7. Ramirez-Alvarado, M., Merkel, J.S., and Regan, L. (2000) A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. USA 97, 8979-8984
8. Chiti, F., Taddei, N., Bucciantini, M., White, P., Ramponi, G., and Dobson C.M. (2000) Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19, 1441-1449
9. Kim, Y., Wall, J.S., Meyer, J., Murphy, C., Randolph, T.W., Manning, M.C., Solomon, A., and Carpenter, J.F. (2000) Thermodynamic modulation of light chain amyloid fibril formation. J. Biol. Chem. 275, 1570-1574
10. Pepys, M.B., Hawkins, P.N., Booth, D.R., Vigushin, D.M., Tennent, G.A., Soutar, A.K., Totty, N., Nguyen, O., Blake, C.C.F., Terry, C.J., Feest, T.G., Zalin, A.M., and Hsuan, J.J. (1993) Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362, 553-557
11. Valleix, S., Drunat, S., Philit, J.B., Adoue, D., Piette, J.C., Droz, D., MacGregor, B., Canet, D., Delpech, M., and Grateau, G. (2002) Hereditary renal amyloidosis caused by a new variant lysozyme W64R in a French family. Kidney Int. 61, 907-912
12. Funahashi, J., Takano, K., Ogasahara, K., Yamagata, Y., and Yutani, K. (1996) The structure, stability, and folding process of amyloidogenic mutant human lysozyme. J. Biochem. 120, 1216-1223
13. Takano, K., Funahashi, J., and Yutani, K. (2001) The stability and folding process of amyloidogenic mutant human lysozymes. Eur J. Biochem. 268, 155-159
14. Goda, S., Takano, K., Yamagata, Y., Katakura, Y., and Yutani, K. (2000) Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. Protein Eng. 13, 299-307
15. Goda, S., Takano, K., Yamagata, Y., Nagata, R., Akutsu, H., Maki, S., Namba, K., and Yutani, K. (2000) Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Protein Sci. 9, 369-375
16. Parry, R.M., Chandan, R.C., and Shahani, K.M. (1969) Isolation and characterization of human milk lysozyme. Arch. Biochem. Biophys. 130, 59-65
17. Sakabe, N. (1991) X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instr Methods. Phys. Res. A303, 448-463
18. Otwinowski, Z. (1990) DENZO Data Processing Package, Yale University, New Haven, CT
19. Brunger, A.T. (1992) X-PLOR Manual, Ver. 3.1, Yale University, New Haven, CT
20. Takano, K., Ogasahara, K., Kaneda, H., Yamagata, Y., Fujii, S., Kanaya, E., Kikuchi, M., Oobatake, M., and Yutani, K. (1995) Contribution of hydrophobic residues to the stability of human lysozyme: Calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J. Mol. Biol. 254, 62-76
21. Yamagata, Y., Kubota, M., Sumikawa, Y., Funahashi, J., Takano, K., Fujii, S., and Yutani, K. (1998) Contribution of hydrogen bonds to the conformational stability of human lysozyme: Calorimetry and X-ray analysis of six Tyr → Phe mutants. Biochemistry 37, 9355-9362
22. Privalov, P.L. and Khechinashvili, N.N. (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study. J. Mol. Biol. 86, 665-684
23. Klunk, W.E., Jacob, R.F., and Mason, R.P. (1999) Quantifying amyloid β-peptide (Aβ) aggregation using the Congo red-Aβ (CR-Aβ) spectrophotomeric assay. Anal. Biochem. 266, 66-76
24. Lashuel, H.A., Lai, Z., and Kelly, J.W. (1998) Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 37, 17851-17864
25. Vonderviszt, F., Sonoyama, M., Tasumi, M., and Namba, K. (1992) Conformational adaptability of the terminal regions of flagellin. Biophys. J. 63, 1672-1677
26. Morozova-Roche, L.A., Zurdo, J., Spencer, A., Noppe, W., Receveur, V., Archer, D.B., Joniau, M., and Dobson, C.M. (2000) Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants. J. Struct. Biol. 130, 339-351
27. Guijarro, J.I., Sunde, M., Jones, J.A., Campbell, I.D., and Dobson, C.M. (1998) Amyloid fibril formation by an SH3 domain. Proc. Natl. Acad. Sci. USA 95, 4224-4228
28. Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., and Dobson, C.M. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. USA 96, 3590-3594
29. Gross, M., Wilkins, D.K., Pitkeathly, M.C., Chung, E.W., Higham, C., Clark, A., and Dobson, C.M. (1999) Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB. Protein Sci. 8, 1350-1357
30. West, M.W., Wang, W., Patterson, J., Mancias, J.D., Beasley, J.R., and Hecht, M.H. (1999) De novo amyloid proteins from designed combinatorial libraries. Proc. Natl. Acad. Sci. USA 96, 11211-11216
31. Yutani, K., Takayama, G., Goda, S., Yamagata, Y., Maki, S., Namba, K., Tsunasawa, S., and Ogasahara, K. (2000) The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus. Biochemistry 39, 2769-2777
32. Krebs, M.R., Wilkins, D.K., Chung, E.W., Pitkeathly, M.C., Chamberlain, A.K., Zurdo, J., Robinson, C.V., and Dobson, C.M. (2000) Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain. J. Mol. Biol. 300, 541-549
33. Canet, D., Last, A.M., Tito, P., Sunde, M., Spencer, A., Archer, D.B., Redfield, C., Robinson, C.V., and Dobson, C.M. (2002) Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nat. Struct. Biol. 9, 308-315
34. Shnyrov, V.L., Villar, E., Zhadan, G.G., Sanchez-Ruiz, J.M., Quintas, A., Saraiva, M.J., and Brito, R.M. (2000) Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin. Biophys. Chem. 88, 61-67
35. Booth, D.R., Sunde, M., Bellotti, V., Robinson, C.V., Hutchinson, W.L., Fraser, P.E., Hawkins, P.N., Dobson, C.M., Radford, S.E., Blake, C.C., and Pepys, M.B. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787-793
36. Litvinovich, S.V., Brew, S.A., Aota, S., Akiyama, S.K., Haudenschild, C., and Ingham, K.C. (1998) Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol. 280, 245-258
37. Bishop, M.F. and Ferrone, F.A. (1984) Kinetics of nucleation-controlled polymerization. A perturbation treatment for use with a secondary pathway. Biophys. J. 46, 631-644.
38. Walsh, D.M., Lomakin, A., Benedek, G.B., Condron, M.M., and Teplow, D.B. (1997) Amyloid β-protein fibrillogenesis. J. Biol. Chem. 272, 22364-22372
39. Lashuel, H.A., Wurth, C., Woo, L., and Kelly, J.W. (1999) The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions. Biochemistry 38, 13560-13573
40. Chiti, F., Taddei, N., Baroni, F., Capanni, C., Stefani, M., Ramponi, G., and Dobson, C.M. (2002) Kinetic partitioning of protein folding and aggregation. Nat. Struct. Biol. 9, 137-143
41. Richardson, J.S. and Richardson, D.C. (2002) Natural β-sheet proteins use negative design to avoid edge-toedge aggregation. Proc. Natl. Acad. Sci. USA 99, 2754-2759
42. Wang, W. and Hecht, M.H. (2002) Rational designed mutations convert de novo amyloid-like fibrils into monomeric β-sheet proteins. Proc. Natl. Acad. Sci. USA 99, 2760-2765