Quantifying the role of chaperones in protein translocation by computational modeling

被引:5
作者
Assenza, Salvatore [1 ]
De Los Rios, Paolo [1 ]
Barducci, Alessandro [1 ]
机构
[1] Ecole Polytech Fed Lausanne, Lab Biophys Stat, Cubotron 723, CH-1015 Lausanne, Switzerland
基金
瑞士国家科学基金会;
关键词
translocation; Hsp70; chaperones; molecular dynamics; free energy;
D O I
10.3389/fmolb.2015.00008
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 molecular chaperone Hsp70 plays a central role in the import of cytoplasmic proteins into organelles, driving their translocation by binding them from the organellar interior. Starting from the experimentally-determined structure of the E. coli Hsp70, we computed, by means of molecular simulations, the effective free-energy profile for substrate translocation upon chaperone binding. We then used the resulting free energy to quantitatively characterize the kinetics of the import process, whose comparison with unassisted translocation highlights the essential role played by Hsp70 in importing cytoplasmic proteins.
引用
收藏
页数:7
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