The prokaryotic thermophilic TF1-ATPase is functionally compatible with the eukaryotic CFo-part of the chloroplast ATP-synthase

Jean Michel Galmiche, Stephane Pezennec, Rongbao Zhao, Guy Girault, Edmund Baeuerlein

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


The ATP synthase from chloroplasts, CFo · F1, was reconstituted into liposomes, from which most of CF1 was removed by a short treatment with guanidinium chloride. ATP-dependent proton uptake was restored with these CFo-liposomes even better by the addition of the bacterial TF1- than of the related CF1-part. This proton uptake was prevented by tentoxin, a specific inhibitor of the CF1-ATPase, in these CFo · F1-liposomes, but not in the hybrid CFo · TF1-liposomes. Venturicidin, a specific inhibitor of proton flow through CFo, was able to block it in both the hybrid CFo· TF1-liposomes and reconstituted CFo· F1-liposomes. These results indicate that the bacterial TF1-part binds to the eukaryotic CFo-part of four subunits forming a functional CFo · TF1-ATPase.

Original languageEnglish (US)
Pages (from-to)152-156
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - Jan 31 1994
Externally publishedYes


  • CF · TF-ATP synthase
  • Functional compatibility
  • Reconstruction (in vitro)
  • Spinach chloroplast
  • Thermophilic bacterium PS3

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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