THE REACTION CYCLE OF GROEL AND GROES IN CHAPERONIN-ASSISTED PROTEIN-FOLDING
THE REACTION CYCLE OF GROEL AND GROES IN CHAPERONIN-ASSISTED PROTEIN-FOLDING
复制标题
DOI：
10.1038/366228a0
复制
发表时间：
1993-11-18
期刊：
影响因子：
64.8
通讯作者：
HARTL, FU
中科院分区：
文献类型：
--
作者：
MARTIN, J;MAYHEW, M;HARTL, FU
蛋白质折叠的伴侣GroEL和它的调节剂GroES的反应机制已被定义。GroES和底物蛋白相互抵消对GroEL的影响：而GroES使GroEL稳定在ADP结合状态，GroEL圆柱体腔内未折叠多肽的结合触发ADP和GroES释放。在ADP-ATP交换后，GroES与GroEL重新结合，ATP水解释放结合的蛋白质进行折叠。部分折叠的蛋白质重新结合到伴侣蛋白上，从而使循环持续下去，直到折叠完成。
The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete.