期刊
FEBS LETTERS
卷 583, 期 7, 页码 1114-1120出版社
WILEY
DOI: 10.1016/j.febslet.2009.02.037
关键词
Stefin B; Amyloid fibril; Proline cis/trans isomerism; Cyclophilin A; Kinetics of fibrillation; Protein-protein interaction
资金
- Slovenian Research Agency [P1-0140, P1-0048]
- Sachsen-Anhalt (Exzellenzcluster Biowissenschaften)
We report that Pro74 in human stefin B is critical for fibril formation and that proline isomerization plays an important role. The stefin B P74S mutant did not fibrillate over the time of observation at 25 degrees C, and it exhibited a prolonged lag phase at 30 degrees C and 37 degrees C. The peptidyl prolyl cis/trans isomerase cyclophilin A, when added to the wild-type protein, exerted two effects: it prolonged the lag phase and increased the yield and length of the fibrils. Addition of the inactive cyclophilin A R55A variant still resulted in a prolonged lag phase but did not mediate the increase of the final fibril yield. These results demonstrate that peptidyl prolyl cis/trans isomerism is rate-limiting in stefin B fibril formation. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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