Axle-Less F1-ATPase Rotates in the Correct Direction

by: Shou Furuike, Mohammad D Hossain, Yasushi Maki, Kengo Adachi, Toshiharu Suzuki, Ayako Kohori, Hiroyasu Itoh, Masasuke Yoshida, Kazuhiko Kinosita

Science, Vol. 319, No. 5865. (15 February 2008), pp. 955-958.

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Abstract

F1adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central gamma subunit rotates inside a cylinder made of three alpha and three subunits alternately arranged. The rotor shaft, an antiparallel alpha-helical coiled coil of the amino and carboxyl termini of the gamma 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. 10.1126/science.1151343

@article{citeulike:2412759, abstract = {F1adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central {gamma} subunit rotates inside a cylinder made of three {alpha} and three subunits alternately arranged. The rotor shaft, an antiparallel {alpha}-helical coiled coil of the amino and carboxyl termini of the {gamma} 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. 10.1126/science.1151343}, author = {Furuike, Shou and Hossain, Mohammad D. and Maki, Yasushi and Adachi, Kengo and Suzuki, Toshiharu and Kohori, Ayako and Itoh, Hiroyasu and Yoshida, Masasuke and Kinosita, Kazuhiko }, citeulike-article-id = {2412759}, doi = {http://dx.doi.org/10.1126/science.1151343}, journal = {Science}, keywords = {experiment, f1-atpase, motor, mutant}, month = {February}, number = {5865}, pages = {955--958}, posted-at = {2008-02-22 10:24:25}, priority = {2}, title = {Axle-Less F1-ATPase Rotates in the Correct Direction}, url = {http://dx.doi.org/10.1126/science.1151343}, volume = {319}, year = {2008} }

RIS record

TY - JOUR ID - citeulike:2412759 L3 - citeulike-article-id:2412759 TI - Axle-Less F1-ATPase Rotates in the Correct Direction JF - Science VL - 319 IS - 5865 SP - 955 EP - 958 N2 - F1adenosine triphosphatase (ATPase) is an ATP-driven rotary molecular motor in which the central {gamma} subunit rotates inside a cylinder made of three {alpha} and three subunits alternately arranged. The rotor shaft, an antiparallel {alpha}-helical coiled coil of the amino and carboxyl termini of the {gamma} 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. 10.1126/science.1151343 KW - experiment KW - f1-atpase KW - motor KW - mutant AU - Furuike, Shou AU - Hossain, Mohammad AU - Maki, Yasushi AU - Adachi, Kengo AU - Suzuki, Toshiharu AU - Kohori, Ayako AU - Itoh, Hiroyasu AU - Yoshida, Masasuke AU - Kinosita, Kazuhiko PY - 2008/02/15/ UR - http://dx.doi.org/10.1126/science.1151343 ER -

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