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.
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.
H
H
Noji
K
K
Häsler
W
W
Junge
K
K
Kinosita
M
M
Yoshida
S
S
Engelbrecht
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