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The prokaryotic thermophilic TF 1 ‐ATPase is functionally compatible with the eukaryotic CF o ‐part of the chloroplast ATP‐synthase
Author(s) -
Galmiche Jean Michel,
Pezennec Stephane,
Zhao Rongbao,
Girault Guy,
Baeuerlein Edmund
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80354-4
Subject(s) - liposome , atp synthase , thermophile , chloroplast , atpase , biochemistry , chemistry , enzyme , gene
The ATP synthase from chloroplasts, CF o · F 1 , was reconstituted into liposomes, from which most of CF 1 was removed by a short treatment with guanidinium chloride. ATP‐dependent proton uptake was restored with these CF o ‐liposomes even better by the addition of the bacterial TF 1 ‐ than of the related CF 1 ‐part. This proton uptake was prevented by tentoxin, a specific inhibitor of the CF 1 ‐ATPase, in these CF o · F 1 ‐liposomes, but not in the hybrid CF o · TF 1 ‐liposomes. Venturicidin, a specific inhibitor of proton flow through CF o , was able to block it in both the hybrid CF o · TF 1 ‐liposomes and reconstituted CF o · F 1 ‐liposomes. These results indicate that the bacterial TF 1 ‐part binds to the eukaryotic CF o ‐part of four subunits forming a functional CF o · TF 1 ‐ATPase.