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