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Isolated ε subunit of Bacillus subtilis F 1 ‐ATPase binds ATP
Author(s) -
Kato-Yamada Yasuyuki
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.036
Subject(s) - bacillus subtilis , atpase , protein subunit , chemistry , adenosine triphosphate , biochemistry , v atpase , enzyme , biophysics , microbiology and biotechnology , biology , bacteria , genetics , gene
Previously, we demonstrated ATP binding to the isolated ε 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 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 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.

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