シャペロニン機能の1分子蛍光イメージング

概要

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Single-molecule imaging is a powerful technique to study functions of biological molecules. As an application of this method, dynamics of the chaperonin (GroEL)-cochaperonin (GroES) interaction and chaperonin-asisited protein folding were visualized by using total internal reflection fluorescence microscopy. Single molecule analysis revealed for the first time that the release of GroES from GroEL was governed by the two successive timers; a lag period (-3s) preceded the net release process (-5s). The protein folding in the immobilized cis complex, monitored using green fluorescent protein and triggered by photolysis of caged-ATP, also started after a lag period (-3s). Thus, the first timer defines the 3s lifetime of a novel intermediate state in which both non-native protein and GroES attach to GroEL. Although increasing number of reports on the observation and analysis of a single protein molecule have been published recently, the study presented here is the first “live-scene” visualization of functional association-dissociation between proteins and of protein folding. The power of this approach will not be restricted in the studies on chaperonin but be extended to the studies on other protein-protein interaction.
社団法人電気学会の論文
2003-04-01