The formation of symmetrical GroEL‐GroES complexes in the presence of ATP

FEBS Letters

Llorca, Oscar¹  Carrascosa, José L.¹  Valpuesta, José M.¹  Marco, Sergio¹ 

[1] Centro Nacional de Biotecnología, CSIC, universidad Autónoma de Madrid, 28049 Madrid, Spain

关键词: Chaperonin;    GroEL—GroES complex;    Protein folding;    Electron microscopy;    Image processing;   

DOI  :  10.1016/0014-5793(94)00432-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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, ATPγS, 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.

【 授权许可】

Unknown