Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging

被引：165

作者：

Adachi, K

Yasuda, R

Noji, H

Itoh, H

Harada, Y

Yoshida, M

Kinosita, K ^{[1
]}

机构：

[1] Genet Programming Team 13, Core Res Evolut Sci & Technol, Miyamae Ku, Kawasaki, Kanagawa 2160001, Japan

[2] Kanazawa Univ, Fac Sci, Dept Phys, Kanazawa, Ishikawa 9201192, Japan

[3] Hamamatsu Photon KK, Tsukuba Res Lab, Tsukuba, Ibaraki 3002635, Japan

[4] Tokyo Inst Technol, Resources Utilizat Res Lab, Midori Ku, Yokohama, Kanagawa 2268503, Japan

[5] Keio Univ, Fac Sci & Technol, Dept Phys, Kohoku Ku, Yokohama, Kanagawa 2238522, Japan

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2000年 / 97卷 / 13期

关键词：

D O I：

10.1073/pnas.120174297

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Orientation dependence of single-fluorophore intensity was exploited in order to videotape conformational changes in a protein machine in real time. The fluorophore Cy3 attached to the central subunit of F-1-ATPase revealed that the subunit rotates in the molecule in discrete 120 degrees steps and that each step is driven by the hydrolysis of one ATP molecule. These results, unlike those from the previous study under a frictional load, show that the 120 degrees stepping is a genuine property of this molecular motor. The data also show that the rate of ATP binding is insensitive to the load exerted on the rotor subunit.

引用

页码：7243 / 7247

页数：5

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