ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.

Junya Mizumoto, Yuka Kikuchi, Yo-Hei Nakanishi, Naoto Mouri, Anrong Cai, Tokushiro Ohta, Takamitsu Haruyama, Yasuyuki Kato-Yamada

PloS one 2013

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MgADP inhibition, which is considered as a part of the regulatory system of ATP synthase, is a well-known process common to all F1-ATPases, a soluble component of ATP synthase. The entrapment of inhibitory MgADP at catalytic sites terminates catalysis. Regulation by the ε subunit is a common mechanism among F1-ATPases from bacteria and plants. The relationship between these two forms of regulatory mechanisms is obscure because it is difficult to distinguish which is active at a particular moment. Here, using F1-ATPase from Bacillus subtilis (BF1), which is strongly affected by MgADP inhibition, we can distinguish MgADP inhibition from regulation by the ε subunit. The ε subunit did not inhibit but activated BF1. We conclude that the ε subunit relieves BF1 from MgADP inhibition.

Citation

Junya Mizumoto, Yuka Kikuchi, Yo-Hei Nakanishi, Naoto Mouri, Anrong Cai, Tokushiro Ohta, Takamitsu Haruyama, Yasuyuki Kato-Yamada. ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition. PloS one. 2013;8(8):e73888