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The formation of symmetrical GroEL‐GroES complexes in the presence of ATP
Author(s) -
Llorca Oscar,
Marco Sergio,
Carrascosa José L.,
Valpuesta José M.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00432-3
Subject(s) - groel , groes , oligomer , chaperonin , chemistry , crystallography , biophysics , biochemistry , biology , protein folding , polymer chemistry , escherichia coli , gene
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.