The intramolecular chaperone-mediated protein folding
The intramolecular chaperone-mediated protein folding
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DOI：
10.1016/j.sbi.2008.10.005
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发表时间：
2008-12-01
影响因子：
6.8
通讯作者：
Inouye, Masayori
中科院分区：
文献类型：
--
作者：
Chen, Yu-Jen;Inouye, Masayori
一些蛋白质已经进化成包含一个特定的序列，作为分子内伴侣，这是蛋白质折叠所必需的，但不是蛋白质功能所必需的，因为它在蛋白质通过自动加工或外源蛋白酶折叠后被移除。到目前为止，大量编码为N-端或C-端延伸的序列已被鉴定为分子内伴侣。越来越多的证据表明，这些分子内伴侣在体内和体外的蛋白质折叠中都发挥着重要的作用。本文综述了近年来分子内伴侣辅助蛋白质折叠的研究进展，并对分子内伴侣在蛋白质折叠中的作用机制进行了讨论。
Some proteins have evolved to contain a specific sequence as an intramolecular chaperone, which is essential for protein folding but not required for protein function, as it is removed after the protein is folded by autoprocessing or by an exogenous protease. To date, a large number of sequences encoded as N-terminal or C-terminal extensions have been identified to function as intramolecular chaperones. An increasing amount of evidence has revealed that these intramolecular chaperones play an important role in protein folding both in vivo and in vitro. Here, we summarize recent studies on intramolecular chaperone-assisted protein folding and discuss the mechanisms as to how intramolecular chaperones play roles in protein folding.