The effects of an ideal β-turn on β-2 microglobulin fold stability

Journal of Biochemistry

Volumn 150, Issue 1, 2011, Pages 39-47

  Colombo, Matteo ^a   Ricagno, Stefano ^a   Barbiroli, Alberto ^a   Santambrogio, Carlo ^b   Giorgetti, Sofia ^c,d   Raimondi, Sara ^c,d   Bonomi, Francesco ^a   Grandori, Rita ^b   Bellotti, Vittorio ^c,d   Bolognesi, Martino ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF MILANO BICOCCA   (Italy)

^c UNIVERSITY OF PAVIA   (Italy)

^d FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

Author keywords

Beta 2 microglobulin; crystal structure; dialysis related amyloidosis; disulphide bond; fold stability

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; CYSTEINE; DISULFIDE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MUTANT PROTEIN; PROLINE;

ARTICLE; BETA SHEET; BETA TURN; CROSS LINKING; CRYSTAL STRUCTURE; DISULFIDE BOND; ELECTROSPRAY MASS SPECTROMETRY; MAJOR HISTOCOMPATIBILITY COMPLEX; MUTATION; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY;

ALZHEIMER DISEASE; AMINO ACID SUBSTITUTION; AMYLOID; AMYLOIDOSIS; BETA 2-MICROGLOBULIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; MUTATION; PROLINE; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY;

EID: 79960097150     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr034     Document Type: Article

References (34)

1. Merlini, G. and Bellotti, V. (2003) Molecular mechanisms of amyloidosis. N. Engl. J. Med. 349, 583-596 (Pubitemid 36951371)
2. Sunde, M., Serpell, L.C., Bartlam, M., Fraser, P.E., Pepys, M.B., and Blake, C.C. (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 273, 729-739
3. Kad, N.M., Myers, S.L., Smith, D.P., Smith, D.A., Radford, S.E., and Thomson, N.H. (2003) Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy. J. Mol. Biol. 330, 785-797
4. Porcelli, S.A. and Modlin, R.L. (1999) The CD1 system: antigen-presenting molecules for T cell recognition of lipids and glycolipids. Annu. Rev. Immunol. 17, 297-329
5. Floege, J. and Ketteler, M. (2001) beta2- microglobulin-derived amyloidosis: an update. Kidney Int. Suppl. 78, S164-S171
6. Gejyo, F., Yamada, T., Odani, S., Nakagawa, Y., Arakawa, M., Kunitomo, T., Kataoka, H., Suzuki, M., Hirasawa, Y., Shirahama, T., Cohen, A.S., and Schimd, K. (1985) A new form of amyloid protein associated with chronic hemodialysis was identified as beta 2-microglobulin. Biochem. Biophys. Res. Commun. 129, 701-706
7. Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F., and Naiki, H. (2004) Glycosaminoglycans enhance the trifluoroethanol- induced extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH. J. Am. Soc. Nephrol. 15, 126-133
8. Esposito, G., Michelutti, R., Verdone, G., Viglino, P., Hernandez, H., Robinson, C.V., Amoresano, A., Dal Piaz, F., Monti, M., Pucci, P., Mangione, P., Stoppini, M., Merlini, G., Ferri, G., and Bellotti, V. (2000) Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9, 831-845
9. Eichner, T. and Radford, S.E. (2009) A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch. J. Mol. Biol. 386, 1312-1326
10. Eakin, C.M., Berman, A.J., and Miranker, A.D. (2006) A native to amyloidogenic transition regulated by a backbone trigger. Nat. Struct. Mol. Biol. 13, 202-208
11. Platt, G.W., Routledge, K.E., Homans, S.W., and Radford, S.E. (2008) Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation. J. Mol. Biol. 378, 251-263
12. Borysik, A.J., Radford, S.E., and Ashcroft, A.E. (2004) Co-populated conformational ensembles of beta2- microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J. Biol. Chem. 279, 27069-27077
13. Mendoza, V.L., Antwi, K., Baron-Rodriguez, M.A., Blanco, C., and Vachet, R.W. (2010) Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry. Biochemistry 49, 1522-1532
14. Smith, D.P., Giles, K., Bateman, R.H., Radford, S.E., and Ashcroft, A.E. (2007) Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometrymass spectrometry. J. Am. Soc. Mass Spectrom. 18, 2180-2190
15. Smith, D.P., Radford, S.E., and Ashcroft, A.E. (2010) Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry. Proc. Natl. Acad. Sci. USA 107, 6794-6798
16. Esposito, G., Ricagno, S., Corazza, A., Rennella, E., Gumral, D., Mimmi, M.C., Betto, E., Pucillo, C.E., Fogolari, F., Viglino, P., Raimondi, S., Giorgetti, S., Bolognesi, B., Merlini, G., Stoppini, M., Bolognesi, M., and Bellotti, V. (2008) The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties. J. Mol. Biol. 378, 885-895
17. Santambrogio, C., Ricagno, S., Colombo, M., Barbiroli, A., Bonomi, F., Bellotti, V., Bolognesi, M., and Grandori, R. (2010) DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form. Protein Sci. 19, 1386-1394
18. Ricagno, S., Colombo, M., de Rosa, M., Sangiovanni, E., Giorgetti, S., Raimondi, S., Bellotti, V., and Bolognesi, M. (2008) DE loop mutations affect beta-2 microglobulin stability and amyloid aggregation. Biochem. Biophys. Res. Commun. 377, 146-150
19. Ricagno, S., Raimondi, S., Giorgetti, S., Bellotti, V., and Bolognesi, M. (2009) Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation. Biochem. Biophys. Res. Commun. 380, 543-547
20. Hutchinson, E.G. and Thornton, J.M. (1994) A revised set of potentials for beta-turn formation in proteins. Protein Sci. 3, 2207-2216
21. Kihara, M., Chatani, E., Iwata, K., Yamamoto, K., Matsuura, T., Nakagawa, A., Naiki, H., and Goto, Y. (2006) Conformation of amyloid fibrils of beta2- microglobulin probed by tryptophan mutagenesis. J. Biol. Chem. 281, 31061-31069
22. Leslie, A.G.W. (1992) Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4ESF-EACMB Newsletter on Protein Crystallography
23. CCP4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 50, 760-763
24. Vagin, A.A. and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025
25. Murshudov, G.N., Vagin, A.A., and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. 53, 240-255
26. Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. 60, 2126-2132
27. Naiki, H., Haschimoto, N., Suzuki, S., Rimura, H., Nakakuki, K., and Gejyo, F. (1997) Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro. AMYLOID: Int. Exp. Clin. Invest. 4, 223-232
28. LeVine, H. III (1993) Thioflavine T interaction with synthetic Alzheimers disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404-410
29. Iwata, K., Matsuura, T., Sakurai, K., Nakagawa, A., and Goto, Y. (2007) High-resolution Crystal Structure of beta2-Microglobulin Formed at pH 7.0. J. Biochem. 142, 413-419
30. Garman, E.F. (2010) Radiation damage in macromolecular crystallography: what is it and why should we care? Acta Crystallogr. 66, 339-351
31. Ohhashi, Y., Hagihara, Y., Kozhukh, G., Hoshino, M., Hasegawa, K., Yamaguchi, I., Naiki, H., and Goto, Y. (2002) 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, 45-52
32. Goto, Y. and Hamaguchi, K. (1979) The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. 86, 1433-1441 (Pubitemid 10217043)
33. Jahn, T.R., Parker, M.J., Homans, S.W., and Radford, S.E. (2006) Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat. Struct. Mol. Biol. 13, 195-201 (Pubitemid 43348504)
34. Sakata, M., Chatani, E., Kameda, A., Sakurai, K., Naiki, H., and Goto, Y. (2008) Kinetic coupling of folding and prolyl isomerization of beta2-microglobulin studied by mutational analysis. J. Mol. Biol. 382, 1242-1255