4.5 Article

Isolated ε subunit of Bacillus subtilis F1-ATPase binds ATP

Journal

FEBS LETTERS
Volume 579, Issue 30, Pages 6875-6878

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2005.11.036

Keywords

ATP binding; regulation; inhibitor; ATP synthase; F0F1

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Previously, we demonstrated ATP binding to the isolated E subunit of F-1-ATPase from thermophilic Bacillus PS3 [Kato-Yamada Y., Yoshida M. (2003) J. Biol. Chem. 278, 36013]. However, whether it is a general feature of the F. subunit from other sources is yet unclear. Here, using a sensitive method to detect weak interactions between fluorescently labeled F subunit and nucleotide, it was shown that the E subunit of F-1-ATPase from Bacillus subtilis also bound ATP. The dissociation constant for ATP binding at room temperature was calculated to be 2 mM, which may be suitable for sensing cellular ATP concentration in vivo. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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