抄録
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.
本文言語 | English |
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ページ(範囲) | 1121-1126 |
ページ数 | 6 |
ジャーナル | FEBS Letters |
巻 | 583 |
号 | 7 |
DOI | |
出版ステータス | Published - 2009 4月 2 |
ASJC Scopus subject areas
- 生化学
- 生物理学
- 細胞生物学
- 遺伝学
- 分子生物学
- 構造生物学