Isolated epsilon subunit of Bacillus subtilis F1-ATPase binds ATP |
| |
Authors: | Kato-Yamada Yasuyuki |
| |
Affiliation: | 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 |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|