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 journalArticlepeer-review

    25 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)1121-1126
    Number of pages6
    JournalFEBS Letters
    Issue number7
    Publication statusPublished - 2009 Apr 2


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

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Cell Biology
    • Genetics
    • Molecular Biology
    • Structural Biology


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