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The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES
Author(s) -
Kawata Yasushi,
Hongo Kunihiro,
Nosaka Koji,
Furutsu Yoshinobu,
Mizobata Tomohiro,
Nagai Jun
Publication year - 1995
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(95)00768-5
Subject(s) - groel , chaperonin , groes , atp hydrolysis , protein folding , biophysics , chemistry , surface plasmon resonance , chaperone (clinical) , biochemistry , adenosine triphosphate , biology , enzyme , escherichia coli , materials science , nanotechnology , medicine , atpase , pathology , nanoparticle , gene
In order to understand the role of ATP hydrolysis of the chaperonin GroEL during protein folding, we have studied GroEL‐GroES complex formation in the presence of ATP or ADP by using capillary electrophoresis and surface plasmon resonance. Capillary electrophoresis analysis showed that the GroEL 14‐mer and GroES 7‐mer formed a 1:1 complex in the presence of ATP. In the presence of ADP, both the association and dissociation rates of the complex were slower by about one order of magnitude than the rates in the presence of ATP at 25°C. The implications of such a stable complex on the overall mechanism of chaperonin function are discussed.