GroEL的耗能分子伴侣机制

双环结构Gro EL及其辅分子伴侣Gro ES是目前研究得最深入的分子伴侣.然而,Gro EL/Gro ES帮助蛋白质折叠的一些关键理化机制,尤其是水解ATP,Gro EL发生构象改变,能否主动调节蛋白质错误折叠中间体的构象,以促进错误折叠中间体的复性,仍然存在争议.结合本研究组近年的工作,作者着力介绍Gro EL促进蛋白质折叠的主动解折叠机制.

GroEL-Assisted Protein Folding by Utilizing The Energy From ATP

The biological function of a protein depends not only on the correct primary amino acid sequence, but also on achieving its native three-dimensional structure. Thus, correct folding of a protein is of great significance to life activities. Due to the complex and crowded intracellular environment, the folding of many proteins is often difficult in vivo. One category of proteins, called chaperones, help other proteins to fold correctly. Chaperones can recognize and stabilize other instable protein to assist its folding. Recent studies showed that, the ring-shaped chaperone GroEL can repetitively unfolding kinetically trapped protein folding intermediate, giving the intermediate another chance to refold, thus increases its overall folding rate. The detailed mechanism of GroEL assisted folding is still under controversy. In this review, we briefly summarize the recent progress in the study of the latter mechanism.