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

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

    Research output: Contribution to journalArticle

    22 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 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
    Volume583
    Issue number7
    DOIs
    Publication statusPublished - 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

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  • Cite this

    Tsumuraya, M., Furuike, S., Adachi, K., Kinosita, K., & Yoshida, M. (2009). Effect of ε subunit on the rotation of thermophilic Bacillus F1-ATPase. FEBS Letters, 583(7), 1121-1126. https://doi.org/10.1016/j.febslet.2009.02.038