THE FORMATION OF SYMMETRICAL GROEL-GROES COMPLEXES IN THE PRESENCE OF ATP

被引：85

作者：

LLORCA, O ^{[1
]}

MARCO, S ^{[1
]}

CARRASCOSA, JL ^{[1
]}

VALPUESTA, JM ^{[1
]}

机构：

[1] UNIV AUTONOMA MADRID,CSIC,CTR NACL BIOTECNOL,E-28049 MADRID,SPAIN

来源：

FEBS LETTERS | 1994年 / 345卷 / 2-3期

关键词：

CHAPERONIN; GROEL-GROES COMPLEX; PROTEIN FOLDING; ELECTRON MICROSCOPY; IMAGE PROCESSING;

D O I：

10.1016/0014-5793(94)00432-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The incubation of chaperonins cpn60 (GroEL) and cpn10 (GroES) from E. coli in the presence of Mg-ATP and KCl generates the formation, as revealed by electron microscopy, of GroEL-GroES complexes with a symmetrical shape in which one toroidal GroES oligomer is bound to each end of the tetradecameric GroEL aggregate (1:2 GroEL:GroES oligomer molar ratio). The symmetrical complexes are not observed in the presence of ADP or the non-hydrolyzable ATP analog, ATP gamma S, where only asymmetrical complexes (1:1 GroEL:GroES oligomer molar ratio) are formed. These results suggest that ATP hydrolysis is required for the formation of symmetrical complexes.

引用

页码：181 / 186

页数：6

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