Rotation of Escherichia coli F-1-ATPase

By applying the same method used for F-1-ATPase (TF,) from thermophilic Bac illus PS3 (Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K., Jr. (1997) Nature 386, 299 -302), we observed ATP-driven rotation of a fluorescent act in filament attached to the gamma subunit in Escherichia coli F-1-ATPase. T he torque value and the direction of the rotation were the same as those ob served for TF1. F-1-ATPases seem to share common properties of rotation irr espective of the sources. (C) 1999 Academic Press.