Aggregation of Partially Unfolded Myosin Subfragment-1 into Spherical Oligomers with Amyloid-Like Dye-Binding Properties

• Published in: Journal of biochemistry (Tokyo) Vol. 139; no. 6; pp. 989 - 996
• Main Authors: Komatsu, Hideyuki, Shinotani, Nami, Kimori, Yoshitaka, Tokuoka, Jun-ichiro, Kaseda, Kuniyoshi, Nakagawa, Hiroyuki, Kodama, Takao
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.06.2006
• Subjects: 3-morpholinopropanesulfonic acid; 4-bis (2-ethanesulfonic acid); amyloid; Amyloid - chemistry; Amyloid - metabolism; Animals; Chromatography, Gel - methods; circular dichroism; Circular Dichroism - methods; Congo Red - chemistry; dithiothreitol; DTT; high performance liquid chromatography; Hot Temperature; HPLC; Kinetics; Microscopy, Electron, Scanning - methods; MOPS; myosin subfragment 1; Myosin Subfragments - chemistry; Myosin Subfragments - metabolism; Myosin Subfragments - ultrastructure; Oligopeptides - chemistry; Oligopeptides - metabolism; partial unfolding; Particle Size; Peptide Fragments - chemistry; Peptide Fragments - metabolism; piperazine-1; PIPES; protein aggregation; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Rabbits; SDS-PAGE; sodium dodecyl sulfate–polyacrylamide gel electrophoresis; Thermodynamics; Thioflavin T; ThioT; Time Factors

Proteolytic myosin subfragment 1 (S1) is known to be partially unfolded in its 50-kDa subdomain by mild heat treatment at 35°C [Burke et al. (1987) Biochemistry 26, 1492-1496]. Here, we report that this partial unfolding is accompanied by aggregation of S1 protein. Characteristics of the aggregate t...