The role of the DELSEED motif of the β subunit in rotation of F1- ATPase

Kiyotaka Y. Hara, Hiroyuki Noji, Dirk Bald, Ryohei Yasuda, Kazuhiko Kinosita, Masasuke Yoshida

研究成果: Article

55 引用 (Scopus)

抜粋

F1-ATPase is a rotary motor protein, and ATP hydrolysis generates torque at the interface between the γ subunit, a rotor shaft, and the α33 substructure, a stator ring. The region of conserved acidic 'DELSEED' motif of the β subunit has a contact with γ subunit and has been assumed to be involved in torque generation. Using the thermophilic α3β3γ complex in which the corresponding sequence is DELSDED, we replaced each residue and all five acidic residues in this sequence with alanine. In addition, each of two conserved residues at the counterpart contact position of γ subunit was also replaced. Surprisingly, all of these mutants rotated with as much torque as the wild-type. We conclude that side chains of the DELSEED motif of the β subunit do not have a direct role in torque generation.

元の言語English
ページ(範囲)14260-14263
ページ数4
ジャーナルJournal of Biological Chemistry
275
発行部数19
DOI
出版物ステータスPublished - 2000 5 12
外部発表Yes

ASJC Scopus subject areas

  • Biochemistry

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    Hara, K. Y., Noji, H., Bald, D., Yasuda, R., Kinosita, K., & Yoshida, M. (2000). The role of the DELSEED motif of the β subunit in rotation of F1- ATPase. Journal of Biological Chemistry, 275(19), 14260-14263. https://doi.org/10.1074/jbc.275.19.14260