By applying the same method used for F1-ATPase (TF1) from thermophilic Bacillus PS3, we observed ATP-driven rotation of a fluorescent actin filament attached to the γ subunit in Escherichia coli F1-ATPase. The torque value and the direction of the rotation were the same as those observed for TF1. F1-ATPases seem to share common properties of rotation irrespective of the sources.
|Number of pages||3|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 1999 Jul 14|
ASJC Scopus subject areas
- Molecular Biology