Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions

被引：3

作者：

He, YB

Tang, HD

Yi, ZW

Zhou, H

Luo, YZ ^{[1
]}

机构：

[1] Tsinghua Univ, Dept Biol Sci & Biotechnol, MOE Lab Prot Sci, Prot Chem Lab, Beijing 100084, Peoples R China

[2] Tsinghua Univ, Dept Biol Sci & Biotechnol, State Key Lab Biomembrane, Beijing 100084, Peoples R China

来源：

FEBS LETTERS | 2005年 / 579卷 / 06期

基金：

中国国家自然科学基金;

关键词：

apomyoglobin; Sup35; aggregation sequence; stability; fibril formation;

D O I：

10.1016/j.febslet.2005.01.059

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：

To examine the effect of aggregation sequence QGGYQQQYNP from yeast Sup35 on fibril formation of sperm whale apomyoglobin (apoMb), we constructed several mutants via substitution. Urea-induced unfolding of apoMb confirms that the substitution of the aggregation sequence does not significantly affect the stability of the mutants compared to wild type (WT) at pH 4.2. Under this condition, however, despite the difference in rate most apoMb mutants form fibrils more readily than WT with distinct morphology. These results suggest that the aggregation sequence facilitates fibril assembly of apoMb at acidic pH in vitro and this facilitation depends on the regions replaced. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1503 / 1508

页数：6

共 28 条

[1] KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF REDUCED POLYPEPTIDE CHAIN [J].