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

研究成果: Article査読

32 被引用数 (Scopus)


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.

ジャーナルBiochemical and Biophysical Research Communications
出版ステータスPublished - 2008 3 14

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

フィンガープリント 「UncI protein can mediate ring-assembly of c-subunits of F<sub>o</sub>F<sub>1</sub>-ATP synthase in vitro」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。