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

doi:10.1016/0014-5793(94)80354-4

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

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

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

The ATP synthase from chloroplasts, CF_o · 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 CF_o-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 CF_o · F₁-liposomes, but not in the hybrid CF_o · TF₁-liposomes. Venturicidin, a specific inhibitor of proton flow through CF_o, was able to block it in both the hybrid CF_o· TF₁-liposomes and reconstituted CF_o· F₁-liposomes. These results indicate that the bacterial TF₁-part binds to the eukaryotic CF_o-part of four subunits forming a functional CF_o · TF₁-ATPase.

Original language	English (US)
Pages (from-to)	152-156
Number of pages	5
Journal	FEBS Letters
Volume	338
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(94)80354-4
State	Published - Jan 31 1994
Externally published	Yes

Keywords

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

Access to Document

10.1016/0014-5793(94)80354-4

Cite this

@article{c6b70a3820764f76a2270eb15a8b09de,

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

abstract = "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.",

keywords = "CF · TF-ATP synthase, Functional compatibility, Reconstruction (in vitro), Spinach chloroplast, Thermophilic bacterium PS3",

author = "Galmiche, {Jean Michel} and Stephane Pezennec and Rongbao Zhao and Guy Girault and Edmund Baeuerlein",

note = "Funding Information: Acknowledgements: We thank the Max Planck Societyf or financial supportt oJ.M.G. and R.Z., the latteri n the exchangep rogramw ith the AcademiaS inica. Beiiina. We also thank PROCOPE, a project relatede xchangeof scientistsbetweeFnra ncea ndG ermanys, ponsored by the Foreign Ministry of France( MAE) and the GermanA cademic ExchangeS ervice( DAAD), for grants,w hich allowedG .G., E.B. and one studento f eachg roup to cooperatein tensivelyw ithin the related laboratoryW. e arev eryg ratefutl o Dr. MasasukeY oshida,Y okohama, for providingu s with a new,f ast growings train of the thermophilic bateriumP S3. We thank Mrs. Seifert-Schillefro r her excellentte chni- cal assistancea nd the preparationo f TF,-ATPase. We thank Mrs. Birnstiel-v.Twardowsfkoi r typingt he manuscript.",

year = "1994",

month = jan,

day = "31",

doi = "10.1016/0014-5793(94)80354-4",

language = "English (US)",

volume = "338",

pages = "152--156",

journal = "FEBS Letters",

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T1 - The prokaryotic thermophilic TF1-ATPase is functionally compatible with the eukaryotic CFo-part of the chloroplast ATP-synthase

AU - Galmiche, Jean Michel

AU - Pezennec, Stephane

AU - Zhao, Rongbao

AU - Girault, Guy

AU - Baeuerlein, Edmund

N1 - Funding Information: Acknowledgements: We thank the Max Planck Societyf or financial supportt oJ.M.G. and R.Z., the latteri n the exchangep rogramw ith the AcademiaS inica. Beiiina. We also thank PROCOPE, a project relatede xchangeof scientistsbetweeFnra ncea ndG ermanys, ponsored by the Foreign Ministry of France( MAE) and the GermanA cademic ExchangeS ervice( DAAD), for grants,w hich allowedG .G., E.B. and one studento f eachg roup to cooperatein tensivelyw ithin the related laboratoryW. e arev eryg ratefutl o Dr. MasasukeY oshida,Y okohama, for providingu s with a new,f ast growings train of the thermophilic bateriumP S3. We thank Mrs. Seifert-Schillefro r her excellentte chni- cal assistancea nd the preparationo f TF,-ATPase. We thank Mrs. Birnstiel-v.Twardowsfkoi r typingt he manuscript.

PY - 1994/1/31

Y1 - 1994/1/31

N2 - 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.

AB - 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.

KW - CF · TF-ATP synthase

KW - Functional compatibility

KW - Reconstruction (in vitro)

KW - Spinach chloroplast

KW - Thermophilic bacterium PS3

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VL - 338

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EP - 156

JO - FEBS Letters

JF - FEBS Letters

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