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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Citations (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.

Original languageEnglish
Pages (from-to)663-666
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 2008 Mar 14
Externally publishedYes


  • ATP synthase
  • Biogenesis of ATP synthase
  • Chaperone
  • In vitro protein synthesis
  • Membrane integration
  • Membrane proteins
  • Motor enzyme
  • UncI
  • YidC
  • c-Subunit

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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