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Facilitated release of substrate protein from prefoldin by chaperonin
Author(s) -
Zako Tamotsu,
Iizuka Ryo,
Okochi Mina,
Nomura Tomoko,
Ueno Taro,
Tadakuma Hisashi,
Yohda Masafumi,
Funatsu Takashi
Publication year - 2005
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/j.febslet.2005.05.061
Subject(s) - chaperonin , biophysics , protein folding , kinetics , chemistry , dissociation (chemistry) , folding (dsp implementation) , chaperone (clinical) , biochemistry , biology , medicine , physics , pathology , quantum mechanics , electrical engineering , engineering
Prefoldin is a chaperone that captures a protein‐folding intermediate and transfers it to the group II chaperonin for correct folding. However, kinetics of interactions between prefoldin and substrate proteins have not been investigated. In this study, dissociation constants and dissociation rate constants of unfolded proteins with prefoldin were firstly measured using fluorescence microscopy. Our results suggest that binding and release of prefoldin from hyperthermophilic archaea with substrate proteins were in a dynamic equilibrium. Interestingly, the release of substrate proteins from prefoldin was facilitated when chaperonin was present, supporting a handoff mechanism of substrate proteins from prefoldin to the chaperonin.