三种伴侣蛋白60s自组装的体外解离：ATP的作用

In vitro dissociation of self-assembly of three chaperonin 60s: the role of ATP.

作者信息

Lissin N M

机构信息

Centre de Biochimie et Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.

出版信息

FEBS Lett. 1995 Mar 13;361(1):55-60. doi: 10.1016/0014-5793(95)00151-x.

DOI:10.1016/0014-5793(95)00151-x

PMID:7890040

Abstract

A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg2+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg2+ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.

摘要

一项比较研究调查了从大肠杆菌（GroEL）、酵母线粒体和豌豆叶绿体中分离出的伴侣蛋白60十四聚体的体外解离和自组装情况。在所有情况下，Mg2+都会抑制尿素诱导的解离，而低温则会刺激这种解离。在Mg2+存在的情况下，ATP或ADP会增强伴侣蛋白的解离。三种蛋白质单体重新组装成十四聚体的效率各不相同。然而，在所有情况下，Mg-腺嘌呤核苷酸都会刺激自组装。令人惊讶的是，在没有ATP的情况下，20%的甘油会促进GroEL的有效自组装。文中讨论了Mg-腺嘌呤核苷酸在伴侣蛋白解离和组装中的作用。