%0 Journal Article
%T ŠĆ Subunit of Bacillus subtilis F1-ATPase Relieves MgADP Inhibition
%A Junya Mizumoto
%A Yuka Kikuchi
%A Yo-Hei Nakanishi
%A Naoto Mouri
%A Anrong Cai
%A Tokushiro Ohta
%A Takamitsu Haruyama
%A Yasuyuki Kato-Yamada
%J PLOS ONE
%D 2013
%I Public Library of Science (PLoS)
%R 10.1371/journal.pone.0073888
%X 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 ŠĆ 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 ŠĆ subunit. The ŠĆ subunit did not inhibit but activated BF1. We conclude that the ŠĆ subunit relieves BF1 from MgADP inhibition.
%U http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0073888