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Literature DB >> 10403811

Rotation of Escherichia coli F(1)-ATPase.

H Noji¹, K Häsler, W Junge, K Kinosita, M Yoshida, S Engelbrecht.

Abstract

By applying the same method used for F(1)-ATPase (TF(1)) 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 TF(1). F(1)-ATPases seem to share common properties of rotation irrespective of the sources. Copyright 1999 Academic Press.

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Year: 1999 PMID： 10403811 DOI： 10.1006/bbrc.1999.0885

Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575

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Cited

24 in total

Review 1. A rotary molecular motor that can work at near 100% efficiency.

Authors: K Kinosita; R Yasuda; H Noji; K Adachi
Journal: Philos Trans R Soc Lond B Biol Sci Date: 2000-04-29 Impact factor: 6.237

2. Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme.

Authors: O Pänke; D A Cherepanov; K Gumbiowski; S Engelbrecht; W Junge
Journal: Biophys J Date: 2001-09 Impact factor: 4.033

3. A biological molecular motor, proton-translocating ATP synthase: multidisciplinary approach for a unique membrane enzyme.

Authors: Y Sambongi; I Ueda; Y Wada; M Futai
Journal: J Bioenerg Biomembr Date: 2000-10 Impact factor: 2.945

Rotation of Escherichia coli F(1)-ATPase.

Review 1. A rotary molecular motor that can work at near 100% efficiency.

2. Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme.

3. A biological molecular motor, proton-translocating ATP synthase: multidisciplinary approach for a unique membrane enzyme.

4. Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase.

5. Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.

6. Activation of pausing F1 motor by external force.

7. Protons, proteins and ATP.

8. The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1-ATPase by the epsilon subunit.

9. Domain compliance and elastic power transmission in rotary F(O)F(1)-ATPase.

10. Two rotary motors in F-ATP synthase are elastically coupled by a flexible rotor and a stiff stator stalk.