The Controlling Roles of Trp60 and Trp95 in β2-Microglobulin Function, Folding and Amyloid Aggregation Properties

Journal of Molecular Biology

Volumn 378, Issue 4, 2008, Pages 887-897

  Esposito, Gennaro ^a   Ricagno, Stefano ^b   Corazza, Alessandra ^a   Rennella, Enrico ^a   Gümral, Devrim ^a   Mimmi, Maria Chiara ^a   Betto, Elena ^a   Pucillo, Carlo E M ^a   Fogolari, Federico ^a   Viglino, Paolo ^a   Raimondi, Sara ^c   Giorgetti, Sofia ^c   Bolognesi, Benedetta ^c   Merlini, Giampaolo ^c,d   Stoppini, Monica ^c   Bolognesi, Martino ^b   Bellotti, Vittorio ^c,d  

^a UNIVERSITY OF UDINE   (Italy)

^b UNIVERSITY OF MILAN   (Italy)

^c UNIVERSITY OF PAVIA   (Italy)

^d FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

Author keywords

amyloid; fibrillogenesis; NMR and X ray structure determination; role of tryptophans in 2 microglobulin; 2 microglobulin

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; LEUKOCYTE ANTIGEN;

AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; HUMAN; HUMAN CELL; MAJOR HISTOCOMPATIBILITY COMPLEX; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; WESTERN BLOTTING;

EID: 41949130213     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.03.002     Document Type: Article

References (51)

1. Merlini G., and Bellotti V. Molecular mechanisms of amyloidosis. N. Engl. J. Med. 349 (2003) 583-596
2. Porcelli S.A., and Modlin R.L. The CD1 system: antigen-presenting molecules for T cell recognition of lipids and glycolipids. Annu. Rev. Immunol. 17 (1999) 297-329
3. Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., and Wiley D.C. Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329 (1987) 506-512
4. 2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci. 11 (2002) 487-499
5. 2-microglobulin. Biochem. Biophys. Res. Commun. 129 (1985) 701-706
6. 2-Microglobulin can be refolded into a native state from ex vivo amyloid fibrils. Eur. J. Biochem. 258 (1998) 61-67
7. 2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9 (2000) 831-845
8. 2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 330 (2003) 785-797
9. 2-microglobulin under physiopathological conditions of dialysis-related amyloidosis. J. Biol. Chem. 281 (2006) 16521-16529
10. 2-microglobulin-related amyloid fibrils at a neutral pH. Biochemistry 43 (2004) 11075-11082
11. 2-microglobulin-related amyloid fibrils at a neutral pH. J. Am. Soc. Nephrol. 15 (2004) 126-133
12. 2-microglobulin fragment are induced by fluorine-substituted alcohols. J. Mol. Biol. 363 (2006) 279-288
13. 2-microglobulin probed by tryptophan mutagenesis. J. Biol. Chem. 281 (2006) 31061-31069
14. Hoshino M., Katou H., Hagihara Y., Hasegawa K., Naiki H., and Goto Y. Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange. Nat. Struct. Biol. 9 (2002) 332-336
15. 2-microglobulin aggregation. Biophys. J. 92 (2007) 1673-1681
16. 2-microglobulin-insights into the mechanism of fibril formation in vitro. J. Mol. Biol. 325 (2003) 249-257
17. 2-microglobulin by Achromobacter protease I. J. Biol. Chem. 277 (2002) 1310-1315
18. 2-microglobulin suggests a molecular model for the fibril. Proc. Natl Acad. Sci. USA 101 (2004) 10584-10589
19. 2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis. J. Biol. Chem. 276 (2001) 46714-46721
20. 2-microglobulin. J. Mol. Biol. 307 (2001) 379-391
21. Naiki H., Haschimoto N., Suzuki S., Rimura H., Nakakuki K., and Gejyo F. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. Amyloid: Int. J. Exp. Clin. Invest. 4 (1997) 223-232
22. 2-Microglobulin H31Y variant 3D structure highlights the protein natural propensity towards intermolecular aggregation. J. Mol. Biol. 335 (2004) 1051-1064
23. Hillig R.C., Hulsmeyer M., Saenger W., Welfle K., Misselwitz R., Welfle H., et al. Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease association. J. Biol. Chem. 279 (2004) 652-663
24. Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
25. 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28 (1989) 8972-8979
26. Garcia de la Torre J., Navarro S., Lopez Martinez M.C., Diaz F.G., and Lopez Cascales J.J. HYDRO: a computer program for the prediction of hydrodynamic properties of macromolecules. Biophys. J. 67 (1994) 530-531
27. 2-microglobulin in solution. Biochemistry 31 (1992) 8906-8915
28. Booth D.R., Sunde M., Bellotti V., Robinson C.V., Hutchinson W.L., Fraser P.E., et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385 (1997) 787-793
29. Batuwangala T., Shepherd D., Gadola S.D., Gibson K.J., Zaccai N.R., Fersht A.R., et al. The crystal structure of human CD1b with a bound bacterial glycolipid. J. Immunol. 172 (2004) 2382-2388
30. 2-microglobulin and amyloidogenesis. J. Biol. Chem. 279 (2004) 9176-9189
31. Lomakin A., Teplow D.B., Kirschner D.A., and Benedek G.B. Kinetic theory of fibrillogenesis of amyloid β-protein. Proc. Natl Acad. Sci. USA 94 (1997) 7942-7947
32. Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., Serpell L., et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289 (2000) 1317-1321
33. Qin Z., Hu D., Zhu M., and Fink A.L. Structural characterization of the partially folded intermediates of an immunoglobulin light chain leading to amyloid fibrillation and amorphous aggregation. Biochemistry 46 (2007) 3521-3531
34. Trinh C.H., Smith D.P., Kalverda A.P., Phillips S.E., and Radford S.E. Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties. Proc. Natl Acad. Sci. USA 99 (2002) 9771-9776
35. 15N NMR relaxation. FEBS Lett. 495 (2001) 52-55
36. LeVine III H. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
37. 2 microglobulin His31Tyr mutant in a tetrameric assembly. Acta Crystallogr., Sect. D: Biol. Crystallogr. 59 (2003) 1270-1272
38. CCP4. The CCP4 Suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
39. Leslie A.G.W. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography 26 (1992)
40. Vagin A.A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
41. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., Sect. D: Biol. Crystallogr. 53 (1997) 240-255
42. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2126-2132
43. Braunschweiler L., and Ernst R.R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53 (1983) 521-528
44. Jeener J., Meier B.H., Bachmann P., and Ernst R.R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71 (1979) 286-292
45. Piantini U., Sorensen O.W., and Ernst R.R. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104 (1982) 6800-6801
46. Bodenhausen G., and Ruben D.J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69 (1980) 185-189
47. 1H]-NMR spectroscopy: combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions. Quart. Rev. Biophys. 23 (1990) 39-96
48. Bax A., and Davis D.G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65 (1985) 355-360
49. Stone M.J., Fairbrother W.J., Palmer III A.G., Reizer J., Saier Jr. M.H., and Wright P.E. Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from nitrogen-15 NMR relaxation measurements. Biochemistry 31 (1992) 4394-4406
50. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113 (1983) 967-974
51. Keeler J., Clowes R.T., Davis A.L., and Laue E.D. Pulsed-field gradients: theory and practice. Methods Enzymol. 239 (1994) 145-207