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Isolated epsilon subunit of Bacillus subtilis F1-ATPase binds ATP
Authors:Kato-Yamada Yasuyuki
Institution:Department of Life Sciences and Frontier Project Life's Adaptation Strategies to Environmental Changes, College of Science, Rikkyo (St. Paul's) University, 3-34-1, Nishi-Ikebukuro, Toshima-ku, Tokyo 171-8501, Japan. katoyama@rikkyo.ac.jp
Abstract:Previously, we demonstrated ATP binding to the isolated epsilon subunit of F1-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 epsilon subunit from other sources is yet unclear. Here, using a sensitive method to detect weak interactions between fluorescently labeled epsilon subunit and nucleotide, it was shown that the epsilon subunit of F1-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.
Keywords:BF1    F1-ATPase from Bacillus subtilis  a soluble portion of FoF1  TF1  F1-ATPase from thermophilic Bacillus PS3  HEPES  2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid  Kd  dissociation constant  NAM  N-(9-acridinyl) maleimide  TMR  tetramethylrhodamine-5-maleimide
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