Effect of ε subunit on the rotation of thermophilic Bacillus F1-ATPase

Masato Tsumuraya; Shou Furuike; Kengo Adachi; Kazuhiko Kinosita; Masasuke Yoshida

doi:10.1016/j.febslet.2009.02.038

Effect of ε subunit on the rotation of thermophilic Bacillus F₁-ATPase

Masato Tsumuraya, Shou Furuike, Kengo Adachi, Kazuhiko Kinosita, Masasuke Yoshida^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

25 Citations (Scopus)

Abstract

F₁-ATPase is an ATP-driven motor in which γε rotates in the α₃β₃-cylinder. It is attenuated by MgADP inhibition and by the ε subunit in an inhibitory form. The non-inhibitory form of ε subunit of thermophilic Bacillus PS3 F₁-ATPase is stabilized by ATP-binding with micromolar K_d at 25 °C. Here, we show that at [ATP] > 2 μM, ε does not affect rotation of PS3 F₁-ATPase but, at 200 nM ATP, ε prolongs the pause of rotation caused by MgADP inhibition while the frequency of the pause is unchanged. It appears that ε undergoes reversible transition to the inhibitory form at [ATP] below K_d.

Original language	English
Pages (from-to)	1121-1126
Number of pages	6
Journal	FEBS Letters
Volume	583
Issue number	7
DOIs	https://doi.org/10.1016/j.febslet.2009.02.038
Publication status	Published - 2009 Apr 2

Keywords

ATP synthase
Epsilon subunit
F
F-ATPase
Motor
Single-molecule

ASJC Scopus subject areas

Biochemistry
Biophysics
Cell Biology
Genetics
Molecular Biology
Structural Biology

Access to Document

10.1016/j.febslet.2009.02.038

Cite this

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abstract = "F1-ATPase is an ATP-driven motor in which γε rotates in the α3β3-cylinder. It is attenuated by MgADP inhibition and by the ε subunit in an inhibitory form. The non-inhibitory form of ε subunit of thermophilic Bacillus PS3 F1-ATPase is stabilized by ATP-binding with micromolar Kd at 25 °C. Here, we show that at [ATP] > 2 μM, ε does not affect rotation of PS3 F1-ATPase but, at 200 nM ATP, ε prolongs the pause of rotation caused by MgADP inhibition while the frequency of the pause is unchanged. It appears that ε undergoes reversible transition to the inhibitory form at [ATP] below Kd.",

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AU - Tsumuraya, Masato

AU - Furuike, Shou

AU - Adachi, Kengo

AU - Kinosita, Kazuhiko

AU - Yoshida, Masasuke

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AB - F1-ATPase is an ATP-driven motor in which γε rotates in the α3β3-cylinder. It is attenuated by MgADP inhibition and by the ε subunit in an inhibitory form. The non-inhibitory form of ε subunit of thermophilic Bacillus PS3 F1-ATPase is stabilized by ATP-binding with micromolar Kd at 25 °C. Here, we show that at [ATP] > 2 μM, ε does not affect rotation of PS3 F1-ATPase but, at 200 nM ATP, ε prolongs the pause of rotation caused by MgADP inhibition while the frequency of the pause is unchanged. It appears that ε undergoes reversible transition to the inhibitory form at [ATP] below Kd.

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