1: J Biol Chem  1998 Jul 31;273(31):19375-7 

Direct observation of the rotation of epsilon subunit in F1-ATPase.

Kato-Yamada Y, Noji H, Yasuda R, Kinosita K Jr, Yoshida M.

Research Laboratory of Resources Utilization, Tokyo Institute of Technology,
4259 Nagatsuta, Yokohama, 226-8503, Japan.

Rotation of the epsilon subunit in F1-ATPase from thermophilic Bacillus strain
PS3 (TF1) was observed under a fluorescence microscope by the method used for
observation of the gamma subunit rotation (Noji, H., Yasuda, R., Yoshida, M.,
and Kinosita, K., Jr. (1997) Nature 386, 299-302). The alpha3 beta3 gamma
epsilon complex of TF1 was fixed to a solid surface, and fluorescently labeled
actin filament was attached to the epsilon subunit through biotin-streptavidin.
In the presence of ATP, the filament attached to epsilon subunit rotated in a
unidirection. The direction of the rotation was the same as that observed for
the gamma subunit. The rotational velocity was slightly slower than the filament
attached to the gamma subunit, probably due to the experimental setup used.
Thus, as suggested from biochemical studies (Aggeler, R., Ogilvie, I. , and
Capaldi, R. A. (1997) J. Biol. Chem. 272, 19621-19624), the epsilon subunit
rotates with the gamma subunit in F1-ATPase during catalysis.

PMID: 9677353 [PubMed - indexed for MEDLINE]