重组蛋白在大肠杆菌中可溶性表达的策略

Strategies for soluble expression of recombinant protein in Escherichia coli

关键词:  重组蛋白  蛋白折叠  分子伴侣  融合标签

Key words:  recombinant protein  protein folding  molecular chaperone  fusion partner

摘要:

重组蛋白技术在许多领域已成为一种必要的工具，但有时表达的目的蛋白却未进行正确的折叠而被蛋白酶降解或聚集形成包涵体。因此，人们在表达不同的目的蛋白时采用了多种方法以期获得具有生物学功能的蛋白质，包括共表达分子伴侣、融合表达、定位表达、改善诱导条件、添加促折叠试剂和选择宿主细胞等。本综述整理了近年来优化蛋白表达的成功经验，从以上方面讨论了如何提高目的蛋白表达的可溶性和促进目的蛋白的正确折叠。

Abstract:

Many recombinant proteins fail to fold into native state with activity when expressed in Escherichia coli, instead, they often misfold and are easy to accumulate as inclusion bodies. Correctly folded recombinant proteins with activity have been obtained through many efficient strategies which include optimization of growing conditions, co-expression of folding modulators, gene fusion expression and so on. Strategies for the solution of the problems in the expression of soluble and bioactive recombinant proteins are discussed in the review.