Essential role of Pro 74 in stefin B amyloid-fibril formation: Dual action of cyclophilin A on the process

被引：18
|
作者：
Smajlovic, Aida [4 ]
Berbic, Selma [4 ]
Schiene-Fischer, Cordelia [3 ]
Tusek-Znidaric, Magda [2 ]
Taler, Ajda [1 ]
Jenko-Kokalj, Sasa [1 ]
Turk, Dusan [1 ]
Zerovnik, Eva [1 ]
机构：
[1] Jozef Stefan Inst, Dept Biochem & Mol Struct Biol, Ljubljana 1000, Slovenia
[2] Natl Inst Biol, Dept Plant Physiol & Biotechnol, Ljubljana 1000, Slovenia
[3] Max Planck Res Unit Enzymol Prot Folding, D-06120 Halle, Saale, Germany
[4] Univ Tuzla, Farmaceut Fac, Dept Biochem, Tuzla 75000, Bosnia & Herceg
来源：
FEBS LETTERS | 2009年 / 583卷 / 07期
关键词：
Stefin B; Amyloid fibril; Proline cis/trans isomerism; Cyclophilin A; Kinetics of fibrillation; Protein-protein interaction; NUCLEAR-MAGNETIC-RESONANCE; ESCHERICHIA-COLI; IN-VITRO; PROTEIN; DOMAIN; CYSTATIN; DISEASE; INTERMEDIATE; AGGREGATION; OLIGOMERS;
D O I：
10.1016/j.febslet.2009.02.037
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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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收藏
页码：1114 / 1120
页数：7
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