分子伴侣协助重组蛋白质高效表达

Research progresses of high-efficient expression of recombinant protein assisted by molecular chaperone

一直以来,具有生物活性的高纯度可溶重组蛋白是蛋白质结构和功能研究的基础,是研究者所期待的目标。但是,在常规表达中异源性重组蛋白往往不能正确折叠为具有生物活性的构象,以致于难以高效表达。本文综述了分子伴侣协助重组蛋白表达的分子机理及其应用现状和所存在的问题,其中涉及分子伴侣的选择原则、蛋白质表达系统与分子伴侣的相关性及相关的改良策略,希望能为合理利用分子伴侣参与重组蛋白表达研究提供借鉴。

Highly purified soluble proteins with bioactivities are the bases for structural and functional studies of protein,and obtaining such samples has long been a desired goal for researchers in the field of molecular and structural biology.However,through usual expression methods,heterologous recombinant proteins are often unable to fold correctly to bioactive conformation,resulting in the difficulties in high-efficient expression.This paper reviews the molecular mechanisms and the current applications of molecular chaperone-assisted expression of recombinant protein.Some existing problems and related solving strategies,including the selection principles of the molecular chaperone and the correlation between protein expression systems and the molecular chaperones,were discussed.Hopefully this review may serve as a reference for rationally utilizing the molecular chaperone in the research of recombinant protein expression.