Role of the N and C-terminal strands of beta 2-microglobulin in amyloid formation at neutral pH

Journal of Molecular Biology

Volumn 330, Issue 5, 2003, Pages 935-941

  Jones, Susan ^a   Smith, David P ^a   Radford, Sheena E ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

Aggregation; Amyloid fibril; Cooperativity; Edge strands; 2 microglobulin

Indexed keywords

ADENINE; AMYLOID; BETA 2 MICROGLOBULIN; FIBRINOGEN VARIANT; GUANINE;

ACIDITY; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION; DNA STRAND; FIBRIN FORMATION; HYDROPHOBICITY; INTERMETHOD COMPARISON; PH MEASUREMENT; POINT MUTATION; PRIORITY JOURNAL;

EID: 0038351889     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00688-0     Document Type: Article

References (38)

1. Hammarström P., Wiseman R.L., Powers E.T., Kelly J.W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science. 299:2003;713-716.
2. Sacchettini J.C., Kelly J.W. Therapeutic strategies for human amyloid diseases. Nature Rev. Drug Discov. 1:2002;267-275.
3. Sittler A., Lurz R., Lueder G., Priller J., Lehrach H., Hayer-Hartl M.K., Hartl F.U., Wanker E.E. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10:2001;1307-1315.
4. Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des. 3:1998;R9-R23.
5. Richardson J.S., Richardson D.C. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl Acad. Sci. USA. 99:2002;2754-2759.
6. Broome B.M., Hecht M.H. Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. J. Mol. Biol. 296:2000;961-968.
7. Wang W., Hecht M.H. Rationally designed mutations convert de novo amyloid-like fibrils into soluble monomeric β-sheet proteins. Proc. Natl Acad. Sci. USA. 99:2002;2760-2765.
8. Mandel-Gutfreund Y., Gregoret L.M. On the significance of alternating patterns of polar and non-polar residues in beta-strands. J. Mol. Biol. 323:2002;453-461.
9. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
10. Rochet J.C., Lansbury P.T. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10:2000;60-68.
11. Lai Z.H., Colon W., Kelly J.W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry. 35:1996;6470-6482.
12. McParland V.J., Kad N.M., Kalverda A.P., Brown A., Kirwin-Jones P., Hunter M.G., et al. Partially unfolded states of beta-2-microglobulin and amyloid formation in vitro. Biochemistry. 39:2000;8735-8746.
13. Khurana R., Gillespie J.R., Talapatra A., Minert L.J., Ionescu-Zanetti C., Millett I., Fink A.L. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry. 40:2001;3525-3535.
14. Ramirez-Alvarado M., Regan L. Does the location of mutations determine the ability to form amyloid fibrils. J. Mol. Biol. 323:2002;17-22.
15. Chiti F., Webster P., Taddei N., Clark A., Stefani M., Ramponi G., Dobson C.M. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl Acad. Sci. USA. 96:1999;3590-3594.
16. Morgan C.J., Gelfand M., Atreya C., Miranker A.D. Kidney dialysis-associated amyloidosis: a molecular role for copper in fibre formation. J. Mol. Biol. 309:2001;339-345.
17. *201/octameric tax peptide complex with an empty conserved peptide-N-terminal binding site. J. Immunol. 164:2000;6398-6405.
18. Trinh C.H., Smith D.P., Kalverda A.P., Phillips S.E., Radford S.E. Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties. Proc. Natl Acad. Sci. USA. 99:2002;9771-9776.
19. Gejyo F., Yamada T., Odani S., Nakagawa Y., Arakawa M., Kunitomo T., et al. A new form of amyloid protein associated with chronic hemodialysis was identified as beta-2-microglobulin. Biochem. Biophys. Res. Commun. 129:1985;701-706.
20. Floege J., Ketteler M. Beta-2-microglobulin-derived amyloidosis: an update. Kidney Int. 59:2001;164-171.
21. Homma N., Gejyo F., Isemura M., Arakawa M. Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis. Nephron. 53:1989;37-40.
22. Smith, D. P., Jones, S., Serpell, L. C., Sunde, M. & Radford, S. E. (2003). A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. J. Mol. Biol. 330, 943-954.
23. McParland V.J., Kalverda A.P., Homans S.W., Radford S.E. Structural properties of an amyloid precursor of beta-2-microglobulin. Nature Struct. Biol. 9:2002;326-331.
24. Katou H., Kanno T., Hoshino M., Hagihara Y., Tanaka H., Kawai T., et al. The role of disulfide bond in the amyloidogenic state of beta 2-microglobulin studied by heteronuclear NMR. Protein Sci. 11:2002;2218-2229.
25. Esposito G., Michelutti R., Verdone G., Viglino P., Hernandez H., Robinson C.V., et al. Removal of the N-terminal hexapeptide from human beta-2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9:2000;831-845.
26. Eakin C.M., Knight J.D., Morgan C.J., Gelfand M.A., Miranker A.D. Formation of a copper specific binding site in non-native states of beta-2-microglobulin. Biochemistry. 41:2002;10646-10656.
27. Kad N.M., Thomson N.H., Smith D.P., Smith D.A., Radford S.E. Beta-2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro. J. Mol. Biol. 313:2001;559-571.
28. Naiki H., Hashimoto N., Suzuki S., Kimura H., Nakakuki K., Gejyo F. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. Amyloid Int. J. Expt. Clin. Invest. 4:1997;223-232.
29. Hoshino M., Katou H., Nakasima Y., Hagihama Y., Hasegawa K., Naiki H., Goto Y. Mapping of the beta-2-microglobulin core by H/D exchange monitored by NMR. Nature Struct. Biol. 9:2002;323-325.
30. Bellotti V., Stoppini M., Mangione P., Sunde M., Robinson C., Asti L., et al. Beta-2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur. J. Biochem. 258:1998;61-67.
31. Kozhukh G.V., Hagihara Y., Kawakami T., Hasegawa K., Naiki H., Goto Y. Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I. J. Biol. Chem. 277:2002;1310-1315.
32. Ohashi Y., Hagihara Y., Kozhukh G., Hoshino M., Hasegawa K., Yamaguchi I., et al. The intrachain disulfide bond of beta-2-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. J. Biochem. 131:2002;45-52.
33. Jones S., Manning J., Kad N.M., Radford S.E. Amyloid-forming peptides from beta 2-microglobulin - insights into the mechanism of fibril formation in vitro. J. Mol. Biol. 325:2003;249-257.
34. Sinha N., Tsai C.J., Nussinov R. A proposed structural model for amyloid fibril elongation: domain swapping forms an interdigitating beta-structure polymer. Protein Eng. 14:2001;93-103.
35. Liu Y., Gotte G., Libonati M., Eisenberg D. A domain-swapped RNase A dimer with implications for amyloid formation. Nature Struct. Biol. 8:2001;211-214.
36. Staniforth R.A., Giannini S., Higgins L.D., Conroy M.J., Hounslow A.M., Jerala R., et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20:2001;4774-4781.
37. Christopher, J. A. (1998). SPOCK: the structural properties observation and calculation kit. (The Center for Macromolecular Design, Texas A & M University, College Station).
38. Chiti F., Mangione P., Andreola A., Giorgetti S., Stefani M., Dobson C.M., et al. Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin. J. Mol. Biol. 307:2001;379-391.