Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053194 | FEBS Letters | 2005 | 4 Pages |
Abstract
Previously, we demonstrated ATP binding to the isolated ε 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 ε subunit from other sources is yet unclear. Here, using a sensitive method to detect weak interactions between fluorescently labeled ε subunit and nucleotide, it was shown that the ε 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.
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Authors
Yasuyuki Kato-Yamada,