Rotation of Escherichia coli F(1)-ATPase.
By applying the same method used for F(1)-ATPase (TF(1)) from thermophilic Bacillus PS3 (Noji, H., Yasuda, R., Yoshida, M., and Kinosita, K., Jr. (1997) Nature 386, 299-302), we observed ATP-driven rotation of a fluorescent actin filament attached to the gamma subunit in Escherichia coli F(1)-ATPase. The torque value and the direction of the rotation were the same as those observed for TF(1). F(1)-ATPases seem to share common properties of rotation irrespective of the sources.
Noji
H
H
CREST team13 (Core Research for Evolutional Science and Technology) "Genetic Programming" Team 13, Teikyo University Biotechnology Research Center 3F, Nogawa 907, Kawasaki, Miyamae-ku, 216-0001, Japan.
Häsler
K
K
Junge
W
W
Kinosita
K
K
Yoshida
M
M
Engelbrecht
S
S
D008841:Actin Cytoskeleton / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D019921:Biotinylation; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008856:Microscopy, Fluorescence; D009154:Mutation; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012399:Rotation; D019809:Streptavidin / Q000378:metabolism; D019415:Torque
D000199:Actins; D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D019809:Streptavidin; D006180:Proton-Translocating ATPases