Single-molecule observation of protein-protein interactions in the chaperonin system.
We have analyzed the dynamics of the chaperonin (GroEL)-cochaperonin (GroES) interaction at the single-molecule level. In the presence of ATP and non-native protein, binding of GroES to the immobilized GroEL occurred at a rate that is consistent with bulk kinetics measurements. However, the release of GroES from GroEL occurred after a lag period ( approximately 3 s) that was not recognized in earlier bulk-phase studies. This observation suggests a new kinetic intermediate in the GroEL-GroES reaction pathway.
Taguchi
H
H
Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226-8503, Japan.
Ueno
T
T
Tadakuma
H
H
Yoshida
M
M
Funatsu
T
T
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D018835:Chaperonin 10 / Q000378:metabolism*; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008856:Microscopy, Fluorescence / Q000379:methods*; D008954:Models, Biological; D015233:Models, Statistical; D011485:Protein Binding; D013552:Swine; D013997:Time Factors
D018835:Chaperonin 10; D000255:Adenosine Triphosphate; D018833:Chaperonins