Formation of amyloid fibrils via longitudinal growth of oligomers

Biochemistry

Volumn 46, Issue 25, 2007, Pages 7365-7373

  Shahi, Puja ^a,b   Sharma, Ritu ^a   Sanger, Shefali ^a   Kumar, Ish ^a,c   Jolly, Ravinder S ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

^b UNIVERSITY OF IOWA   (United States)

^c WESLEYAN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; ETHANOL; GROWTH KINETICS; MOLECULAR STRUCTURE; SOLUTIONS; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID FIBRILS; ETHANOL SOLUTION; THIOESTERASE;

OLIGOMERS;

ALCOHOL; AMYLOID; BACTERIAL ENZYME; OLIGOMER; PROTEIN SUBUNIT; THIOL ESTER HYDROLASE;

ALCALIGENES FAECALIS; ARTICLE; BETA SHEET; CONTROLLED STUDY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS; TRANSMISSION ELECTRON MICROSCOPY;

ALCALIGENES FAECALIS; AMYLOID; BACTERIAL PROTEINS; BIREFRINGENCE; BUFFERS; CIRCULAR DICHROISM; COENZYME A-TRANSFERASES; ETHANOL; HYDROGEN-ION CONCENTRATION; MOLECULAR WEIGHT; PHOSPHATES; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; TEMPERATURE; TIME FACTORS;

ALCALIGENES FAECALIS;

EID: 34250808419     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7001136     Document Type: Article

References (46)

1. Stefani, M., and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution, J. Mol. Med. 81, 678-699.
2. Ehud, G. (2005) Mechanisms of amyloid fibril self-assembly and inhibition by model short peptides as a key research tool, FEBS J, 272, 5971-5978.
3. Rochet, J. C., and Lansbury, P. T., Jr. (2000) Amyloid fibrillogenesis: Themes and variations, Curr. Opin. Struct. Biol. 10, 60-68.
4. Serpell, L. C. (2000) Alzheimer's amyloid fibrils: Structure and assembly, Biochim. Biophys. Acta 1502, 16-30.
5. 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. U.S.A. 95, 4224-4228.
6. 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.
7. 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.
8. Chapman, M. R., Robinson, L. S., Pinkner, J. S., Roth, R., Heuser, J., Hammar, M., Normark, S., and Hultgren, S. J. (2002) Role of Escherichia coli curli operons in directing amyloid fiber formation, Science 295, 851-855.
9. Claessen, D., Rink, R., de Jong, W., Siebring, J., de Vreugd, P., Boersma, F. G., Dijkhuizen, L., and Wosten, H. A. (2003) A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils, Genes Dev. 17, 1714-1726.
10. Gebbink, M. F., Claessen, D., Bouma, B., Dijkhuizen, L., and Wosten, H. A. (2005) Amyloids: A functional coat for microorganisms, Nat. Rev. Microbiol. 3, 333-341.
11. Goldsbury, C. S., Cooper, G. J., Goldie, K. N., Muller, S. A., Saafi, E. L., Gruijters, W. T., Misur, M. P., Engel, A., Aebi, U., and Kistler, J. (1997) Polymorphic fibrillar assembly of human amylin, J. Struct. Biol. 119, 17-27.
12. Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T. (1997) Observation of metastable Aβ amyloid protofibrils by atomic force microscopy, Chem. Biol. 4, 119-125.
13. Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., and Teplow, D. B. (1999) Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates, J. Biol. Chem. 274, 25945-25952.
14. Goldsbury, C., Kistler, J., Aebi, U., Arvinte, T., and Cooper, G. J. (1999) Watching amyloid fibrils grow by time-lapse atomic force microscopy, J. Mol. Biol. 285, 33-39.
15. Green, J. D., Goldsbury, C., Kistler, J., Cooper, G. J., and Aebi, U. (2004) Human amylin oligomer growth and fibril elongation define two distinct phases in amyloid formation, J. Biol. Chem. 279, 12206-12212.
16. Shahi, P., Kumar, I., Sharma, R., Sangar, S., and Jolly, R. S. (2006) Characterization of a novel long-chain acyl-coA thioesterase from Alcaligenes faecalis, FEBS J. 273, 2374-2387.
17. Kumar, I., and Jolly, R. S. (2001) A thioesterase for chemoselective hydrolysis of S-acyl sulfanylalkanoates, Org. Lett. 3, 283-285.
18. Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., and Rydel, R. E. (2005) Nucleation-Dependent Polymerization Is an Essential Component of Amyloid-Mediated Neuronal Cell Death, J. Neurosci. 25, 1071-1080.
19. Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., and Stefani, M. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases, Nature 416, 507-511.
20. Barnes, E. M., Jr., and Wakil, S. J. (1968) Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmitoyl thioesterase, J. Biol. Chem. 243, 2955-2962.
21. Klunk, W. E., Jacob, R. F., and Mason, R. P. (1999) Quantifying amyloid by congo red spectral shift assay, Methods Enzymol. 309, 285-305.
22. Klunk, W. E., Pettegrew, J. W., and Abraham, D. J. (1989) Quantitative evaluation of congo red binding to amyloid-like proteins with a β-pleated sheet conformation, J. Histochem. Cytochem. 37, 1273-1281.
23. LeVine, H., III (1995) Thioflavin T interaction with amyloid β sheet structure, Amyloid: Int. J. Exp. Clin. Invest. 2, 1-6.
24. Chiti, F., Bucciantini, M., Capanni, C., Taddei, N., Dobson, C. M., and Stefani, M. (2001) Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain, Protein Sci. 10, 2541-2547.
25. Kelly, J. W. (1998) The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways, Curr. Opin. Struct. Biol. 8, 101-106.
26. Jarret, J. T., and Lansbury, P. T., Jr. (1993) Seeding the one-dimensional crystallization of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
27. Soreghan, B. J. K., and Glabe, C. (1994) Surfactant properties of Alzheimer's Aβ peptides and the mechanism of amyloid aggregation, J. Biol. Chem. 269, 28551-28554.
28. Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., and Teplow, D. B. (1996) On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants, Proc. Natl. Acad. Sci. U.S.A. 93, 1125-1129.
29. Harper, J. D., and Lansbury, P. T., Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins, Annu. Rev. Biochem. 66, 385-407.
30. Bitan, G., and Teplow, D. B. (2004) Rapid photochemical cross-linking: A new tool for studies of metastable, amyloidogenic protein assemblies, Acc. Chem. Res. 37, 357-364.
31. Mousseau, M., and Derreumaux, P. (2005) Exploring the Early Steps of Amyloid Peptide Aggregation by Computers, Acc. Chem. Res. 38, 885-891.
32. Cecchini, M., Curcio, R., Pappalardo, M., Melki, R., and Caflisch, A. (2006) A Molecular Dynamics Approach to the Structural Characterization of Amyloid Aggregation, J. Mol. Biol. 357, 1306-1321.
33. Lopez de la Paz, M., and Serrano, L. (2004) Sequence determinants of amyloid fibril formation, Proc. Natl. Acad. Sci. U.S.A. 101, 87-92.
34. Eigen, M. (1996) Prionics or the kinetic basis of prion diseases, Biophys. Chem. 63, A1-A18.
35. Durbin, S. D., and Feher, G. (1996) Protein crystallization, Annu. Rev. Phys. Chem. 47, 171-204.
36. Bader, R., Bamford, R., Zurdo, J., Luisi, B. F., and Dobson, C. M. (2006) Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation, J. Mol. Biol. 356, 189-208.
37. Cinelli, S., Onori, G., and Santucci, A. (1999) Effect of 1-alcohols on micelle formation and protein folding, Colloids Surf., A 160, 3-8.
38. Ruiz-Pena, M., Comas-Rojas, H., Rodriguez-Calvo, S., and Perez-Gramatges, A. (2005) Self-association behaviour of protein: surfactant systems in alcohol/water mixtures, Nanobiotechnol., IEEE Proc. 152, 177-181.
39. Krzaczkowska, J., Gierszewski, J., and Slosarek, G. (2004) Solubility of adenine and kinetin in water-ethanol solutions, J. Solution Chem. 33, 395-340.
40. Amo, Y., and Tominaga, Y. (2000) Low-frequency Raman study of ethanol-water mixture, Chem. Phys. Lett. 320, 703.
41. Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., et al. (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant, Science 289, 1317-1321.
42. San Biagio, P. L., Martorana, V., Emanuele, A., Vaiana, S. M., Manno, M., Bulone, D., et al. (1999) Interacting processes in protein coagulation, Proteins: Struct., Funct., Genet. 37, 116-120.
43. Gregoire, C., Marco, S., Thimonier, J., Duplan, L., Laurine, E., Chauvin, J.-P., Michel, B., Peyrot, V., and Verdier, J.-M. (2001) Three dimensional structure of the lithostathine protofilament, a protein involved in Alzheimer's disease, EMBO J. 20, 3313-3321.
44. Chiti, F., Bucciantini, M., Capanni, C., Taddei, N., Dobson, C. M., and Stefani, M. (2001) Solution conditions can promote formation of either amyloid protofi laments or mature fibrils from the HypF N-terminal domain, Protein Sci. 10, 2541-2547.
45. Dixit, S., Crain, J., Poon, W. C. K., Finney, J. L., and Soper, A. K. (2002) Molecular segregation observed in a concentrated alcohol-water solution, Nature 416, 829-831.
46. Gómez-Ramos, P., and Moran, M. A. (2007) Ultrastructural localization of intraneuronal Aβ-peptide in alzheimer disease brains, J. Alzheimer's Dis. 11, 53-59.