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.

引用

页码：1114 / 1120

页数：7

共 13 条

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