The Regions of the Sequence Most Exposed to the Solvent Within the Amyloidogenic State of a Protein Initiate the Aggregation Process

Journal of Molecular Biology

Volumn 336, Issue 1, 2004, Pages 253-262

  Monti, Maria ^a   Garolla Di Bard, Barbara Lelj ^a   Calloni, Giulia ^b   Chiti, Fabrizio ^b   Amoresano, Angela ^a   Ramponi, Gianpietro ^b   Pucci, Piero ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Acylphosphatase; Aggregation; Amyloid; Limited proteolysis; Mass spectrometry

Indexed keywords

ACYLPHOSPHATASE; AMYLOID; PROTEINASE; TRIFLUOROETHANOL;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ELECTROSPRAY; ESCHERICHIA COLI; LIGAND BINDING; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN ENGINEERING; PROTEIN FOLDING;

EID: 0346500469     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.082     Document Type: Article

References (36)

1. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
2. Guijarro J.I., Sunde M., Jones J.A., Campbell I.D., Dobson C.M. Amyloid fibril formation by an SH3 domain. Proc. Natl Acad. Sci. USA. 95:1998;4224-4228.
3. Litvinovich S.V., Brew S.A., Aota S., Akiyama S.K., Haudenschild C., Ingham K.C. Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol. 280:1998;245-258.
4. 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.
5. Konno T., Murata K., Nagayama K. Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin. FEBS Letters. 454:1999;122-126.
6. Kallberg Y., Gustafsson M., Persson B., Thyberg J., Johansson J. Prediction of amyloid fibril-forming proteins. J. Biol. Chem. 276:2001;12945-12950.
7. Yutani K., Takayama G., Goda S., Yamagata Y., Maki S., Namba K., et al. The process of amyloid-like fibril formation by methionine aminopeptidase from a hyperthermophile, Pyrococcus furiosus. Biochemistry. 39:2000;2769-2777.
8. Ramirez-Alvarado M., Merkel J.S., Regan L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl Acad. Sci. USA. 97:2000;8979-8984.
9. Kallijarvi J., Haltia M., Baumann M.H. Amphoterin includes a sequence motif which is homologous to the Alzheimer's beta-amyloid peptide (Abeta), forms amyloid fibrils in vitro, and binds avidly to Abeta. Biochemistry. 40:2001;10032-10037.
10. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511.
11. Eliezer D., Chiba K., Tsuruta H., Doniach S., Hodgson K.O., Kihara H. Evidence of an associative intermediate on the myoglobin refolding pathway. Biophys. J. 65:1993;912-917.
12. Silow M., Oliveberg M. High-energy channeling in protein folding. Biochemistry. 36:1997;7633-7637.
13. Silow M., Tan Y.J., Fersht A.R., Oliveberg M. Formation of short-lived protein aggregates directly from the coil in two-state folding. Biochemistry. 38:1999;13006-13012.
14. van den Berg B., Ellis R.J., Dobson C.M. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18:1999;6927-6933.
15. McParland V.J., Kalverda A.P., Homans S.W., Radford S.E. Structural properties of an amyloid precursor of β2-microglobulin. Nature Struct. Biol. 9:2002;326-331.
16. Wood S.J., Wetzel R., Martin J.D., Hurle M.R. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4. Biochemistry. 34:1995;724-730.
17. Moriarty D.F., Raleigh D.P. Effects of sequential proline substitutions on amyloid formation by human amylin 20-29. Biochemistry. 38:1999;1811-1818.
18. Tjernberg L.O., Callaway D.J., Tjernberg A., Hahne S., Lilliehook C., Terenius L., et al. A molecular model of Alzheimer amyloid beta-peptide fibril formation. J. Biol. Chem. 274:1999;12619-12625.
19. Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G., Dobson C.M. Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol. 9:2002;137-143.
20. Orrù S., Dal Piaz F., Casbarra A., Biasiol G., De Francesco R., Steinkuhler C., Pucci P. Conformational changes in the NS3 protease from hepatitis C virus strain BK monitored by limited proteolysis and mass spectrometry. Protein Sci. 8:1999;1445-1454.
21. Bianchi E., Orrù S., Dal Piaz F., Ingenito R., Casbarra A., Biasiol G., et al. Conformational changes in human hepatitis virus NS3 protease upon binding of product-based inhibitors. Biochemistry. 38:1999;13844-13852.
22. Piccoli R., De Lorenzo C., Dal Piaz F., Pucci P., D'Alessio G. Trypsin sheds light on the singular case of seminal rnase, a dimer with two quaternary conformations. J. Biol. Chem. 275:2000;8000-8006.
23. Esposito G., Michelutti R., Verdone G., Viglino P., Hernandez H., Robinson C.V., et al. Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci. 9:2000;831-845.
24. * partly folded intermediate of wild-type and P138A EcAspAT. J. Biol. Chem. 277:2002;17428-17437.
25. Modesti A., Taddei N., Bucciantini M., Stefani M., Colombini B., Raugei G., Ramponi G. Expression, purification, and characterization of acylphosphatase muscular isoenzyme as fusion protein with glutathione S-transferase. Protein Expr. Purif. 6:1995;799-805.
26. van Nuland N.A., Chiti F., Taddei N., Raugei G., Ramponi G., Dobson C.M. Slow folding of muscle acylphosphatase in the absence of intermediates. J. Mol. Biol. 283:1998;883-891.
27. Pastore A., Saudek V., Ramponi G., Williams R.J. Three-dimensional structure of acylphosphatase. Refinement and structure analysis. J. Mol. Biol. 224:1992;427-440.
28. Chiti F., Taddei N., Webster P., Hamada D., Fiaschi T., Ramponi G., Dobson C.M. Acceleration of the folding of acylphosphatase by stabilization of local secondary structure. Nature Struct. Biol. 6:1999;380-387.
29. Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature. 418:2002;291.
30. Stefani M., Taddei N., Ramponi G. Insights into acylphosphatase structure and catalytic mechanism. Cell. Mol. Life Sci. 53:1997;141-151.
31. Baures P.W., Peterson S.A., Kelly J.W. Discovering transthyretin amyloid fibril inhibitors by limited screening. Bioorg. Med. Chem. 6:1998;1389-1401.
32. Chiti F., Taddei N., Stefani M., Dobson C.M., Ramponi G. Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. Protein Sci. 10:2001;879-886.
33. Zappacosta F., Pessi A., Bianchi E., Venturini S., Sollazzo M., Tramontano A., et al. Probing the tertiary structure of proteins by limited proteolysis and mass spectrometry: the case of Minibody. Protein Sci. 5:1996;802-813.
34. Chiti F., Taddei N., White P.M., Bucciantini M., Magherini F., Stefani M., Dobson C.M. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nature Struct. Biol. 6:1999;1005-1009.
35. Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295:2002;1852-1858.
36. Rudiger S., Germeroth L., Schneider-Mergener J., Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16:1997;1501-1507.