Fast folding of the two-domain Semliki forest virus capsid protein explains co-translational proteolytic activity

被引:31
作者
Sánchez, IE
Morillas, M
Zobeley, E
Kiefhaber, T
Glockshuber, R
机构
[1] Univ Basel, Biozentrum, Biophys Chem Abt, CH-4056 Basel, Switzerland
[2] ETH Honggerberg, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland
关键词
protein folding; co-translational folding; semliki Forest virus protease; two-domain proteins; prolyl isomerization;
D O I
10.1016/j.jmb.2004.02.037
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
The capsid protein of Semliki Forest virus constitutes the N-terminal part of a large viral polyprotein. It consists of an unstructured basic segment (residues 1-118) and a 149 residue serine protease module (SFVP, residues 119-267) comprised of two P-barrel domains. Previous in vivo and in vitro translation experiments have demonstrated that SFVP folds co-translationally during synthesis of the viral polyprotein and rapidly cleaves itself off the nascent chain. To test whether fast co-translation folding of SFVP is an intrinsic property of the polypeptide chain or whether folding is accelerated by cellular components, we investigated spontaneous folding of recombinant SFVP in vitro. The results show that the majority of unfolded SFVP molecules fold faster than any previously studied two-domain protein (tau = 50 ms), and that folding of the N-terminal domain precedes structure formation of the C-terminal domain. This shows that co-translational folding of SFVP does not require additional cellular components and suggests that rapid folding is the result of molecular evolution towards efficient virus biogenesis. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:159 / 167
页数:9
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