Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation.
F0F1, found in mitochondria or bacterial membranes, synthesizes adenosine 5'-triphosphate (ATP) coupling with an electrochemical proton gradient and also reversibly hydrolyzes ATP to form the gradient. An actin filament connected to a c subunit oligomer of F0 was able to rotate by using the energy of ATP hydrolysis. The rotary torque produced by the c subunit oligomer reached about 40 piconewton-nanometers, which is similar to that generated by the gamma subunit in the F1 motor. These results suggest that the gamma and c subunits rotate together during ATP hydrolysis and synthesis. Thus, coupled rotation may be essential for energy coupling between proton transport through F0 and ATP hydrolysis or synthesis in F1.
Sambongi
Y
Y
Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation, Ibaraki, Osaka 567-0047, Japan.
Iko
Y
Y
Tanabe
M
M
Omote
H
H
Iwamoto-Kihara
A
A
Ueda
I
I
Yanagida
T
T
Wada
Y
Y
Futai
M
M
D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D001665:Binding Sites; D019921:Biotinylation; D004735:Energy Transfer; D004800:Enzymes, Immobilized; D004926:Escherichia coli / Q000201:enzymology; D006868:Hydrolysis; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D018892:Proton-Motive Force; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D014475:Uncoupling Agents / Q000378:metabolism / Q000494:pharmacology; D014698:Venturicidins / Q000494:pharmacology; D014741:Video Recording
D000199:Actins; D004800:Enzymes, Immobilized; D020409:Molecular Motor Proteins; D014475:Uncoupling Agents; D014698:Venturicidins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases