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ABSTRACT:
SUBMITTER: Sameshima T
PROVIDER: S-EPMC3259762 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
Sameshima Tomoya T Ueno Taro T Iizuka Ryo R Ishii Noriyuki N Terada Naofumi N Okabe Kohki K Funatsu Takashi T
The Journal of biological chemistry 20080620 35
GroEL is an Escherichia coli chaperonin that is composed of two heptameric rings stacked back-to-back. GroEL assists protein folding with its cochaperonin GroES in an ATP-dependent manner in vitro and in vivo. However, it is still unclear whether GroES binds to both rings of GroEL simultaneously under physiological conditions. In this study, we monitored the GroEL-GroES interaction in the reaction cycle using fluorescence resonance energy transfer. We found that nearly equivalent amounts of symm ...[more]