IN-VITRO DISSOCIATION AND SELF-ASSEMBLY OF 3 CHAPERONIN-60S - THE ROLE OF ATP
IN-VITRO DISSOCIATION AND SELF-ASSEMBLY OF 3 CHAPERONIN-60S - THE ROLE OF ATP
复制标题
DOI：
10.1016/0014-5793(95)00151-x
复制
发表时间：
1995-03-13
期刊：
影响因子：
3.5
通讯作者：
LISSIN, NM
中科院分区：
文献类型：
--
作者：
LISSIN, NM
比较研究了从大肠杆菌中分离的伴侣蛋白60的体外解离和自组装。在所有情况下，Mg ~（2+）抑制尿素诱导的解离，而低温刺激尿素诱导的解离。ATP或ADP在Mg ~（2+）存在下增强了伴侣蛋白的解离。从其单体的14聚体的重新组装显示三种蛋白质之间的不同效率。然而，在所有情况下，自组装是由镁腺嘌呤核苷酸刺激。令人惊讶的是，在不存在ATP的情况下，20%甘油可以促进GroEL的有效自组装。镁-腺嘌呤核苷酸的解离和组装的伴侣蛋白的作用进行了讨论。
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.