共 13 条
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
收藏
页码:1114 / 1120
页数:7
相关论文