UncI protein can mediate ring-assembly of c-subunits of FoF1-ATP synthase in vitro

Yoko Ozaki, Toshiharu Suzuki, Yutetsu Kuruma, Takuya Ueda, Masasuke Yoshida*

*この研究の対応する著者

研究成果: Article査読

32 被引用数 (Scopus)

抄録

In FoF1-ATP synthase, multimeric c-subunits are assembled to a ring (c-ring) in the membranes that rotates as protons flow across Fo. We recently reported that assembly of c-ring of Propionigenium modestum in the membranes of Escherichia coli cells required P. modestum UncI, a product of the conserved uncI gene in the FoF1 operon. However, cooperation with endogenous factors in E. coli remained unclear. Here, P. modestum c-subunit was synthesized in vitro in the presence of liposomes. When c-subunit alone was synthesized, it did not form c-ring. However, when c-subunit and P. modestum UncI were synthesized together, c-ring was formed. Fusion of the two kinds of liposomes, one containing only unassembled c-subunit and the other only UncI, resulted in gradual formation of c-ring. Thus, UncI alone can mediate in vitro post-translational c-ring assembly.

本文言語English
ページ(範囲)663-666
ページ数4
ジャーナルBiochemical and Biophysical Research Communications
367
3
DOI
出版ステータスPublished - 2008 3 14
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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