Rotation of Escherichia coli F1-ATPase

被引:77
作者
Noji, H
Häsler, K
Junge, W
Kinosita, K
Yoshida, M [1 ]
Engelbrecht, S
机构
[1] Tokyo Inst Technol, Resources Utilizat Res Lab, Yokohama, Kanagawa 2268508, Japan
[2] Keio Univ, Fac Sci & Technol, Yokohama, Kanagawa 2238522, Japan
[3] Univ Osnabruck, Fachbereich Biol Chem, Biophys Abt, D-49069 Osnabruck, Germany
[4] Teikyo Univ, Biotechnol Res Ctr 3F, Genet Programming Team 13, Core Res Evolut Sci & Technol,Miyamae Ku, Kawasaki, Kanagawa 2160001, Japan
关键词
D O I
10.1006/bbrc.1999.0885
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
By applying the same method used for F-1-ATPase (TF,) 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 TF1. F-1-ATPases seem to share common properties of rotation irrespective of the sources. (C) 1999 Academic Press.
引用
收藏
页码:597 / 599
页数:3
相关论文
共 14 条
  • [11] PHILLIP HK, 1998, FEBS LETT, V426, P217
  • [12] Intersubunit rotation in active F-ATPase
    Sabbert, D
    Engelbrecht, S
    Junge, W
    [J]. NATURE, 1996, 381 (6583) : 623 - 625
  • [13] WISE JG, 1990, J BIOL CHEM, V265, P10403
  • [14] F1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    Yasuda, R
    Noji, H
    Kinosita, K
    Yoshida, M
    [J]. CELL, 1998, 93 (07) : 1117 - 1124