Jump to: Page Content, Section Navigation, Site Navigation, Site Search, Account Information, or Site Tools.
|
|
ReportsAxle-Less F1-ATPase Rotates in the Correct Direction![]()
F1–adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central
1 Department of Physics, Faculty of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo 169-8555, Japan. subunit rotates inside a cylinder made of three and three β subunits alternately arranged. The rotor shaft, an antiparallel -helical coiled coil of the amino and carboxyl termini of the subunit, deeply penetrates the central cavity of the stator cylinder. We truncated the shaft step by step until the remaining rotor head would be outside the cavity and simply sat on the concave entrance of the stator orifice. All truncation mutants rotated in the correct direction, implying torque generation, although the average rotary speeds were low and short mutants exhibited moments of irregular motion. Neither a fixed pivot nor a rigid axle was needed for rotation of F1-ATPase.
2 Department of Physics, School of Physical Sciences, Shahjalal University of Science and Technology, Sylhet-3114, Bangladesh. 3 Department of Physics, Osaka Medical College, Osaka 569-8686, Japan. 4 Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan. 5 ATP-Synthesis Regulation Project, International Cooperative Research Project (ICORP), Japan Science and Technology Agency (JST), Aomi 2-41, Tokyo 135-0064, Japan. 6 Tsukuba Research Laboratory, Hamamatsu Photonics KK, Tokodai, Tsukuba 300-2635, Japan. 7 Core Research for Evolutional Science and Technology (CREST) "Formation of Soft Nano-Machines" Team 13*, Tokodai, Tsukuba 300-2635, Japan. * These authors contributed equally to this work.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
|
Science. ISSN 0036-8075 (print), 1095-9203 (online)