F0 and F1 parts of ATP synthases from Clostridium thermoautotrophicum and Escherichia coli are not functionally compatible

FEBS Letters

Ljungdahl, Lars G.¹  Das, Amaresh¹ 

[1] Center for Biological Resource Recovery and Department of Biochemistry, University of Georgia, Athens, GA 30602, USA

关键词: Clostridium thermoautotrophicum;    Escherichia coli;    F1F0-ATP synthase;    In vitro reconstitution;    Functional compatibility;    SDS;    sodium dodecyl sulfate;    DCCD;    N-N-dicyclohexylcarbodimide;    PMSF;    phenylmethylsulfonyl fluoride;    ANS;    anilinonaphthalene sulfonate;   

DOI  :  10.1016/0014-5793(93)81482-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

F₁-stripped membrane vesicles from Clostridium thermoautotrophicum and Escherichia coli were reconstituted with F₁-ATPases from both bacteria. Reconstituted F_iF_o-ATPase complexes were catalytically active, i.e. capable of hydrolyzing ATP. Homologous-type ATPase complexes having F₀ and F₁ parts of ATP synthases from the same origin were DCCD sensitive and supported ATP-driven enhancement ofanilinonaphthalene sulfonate (ANS) fluorescence. Hybrid-type ATPase complexes having F₀ and F₁ parts of ATP synthases from different origins were neither DCCD sensitive nor did they support ATP-driven enhancement of ANS fluorescence. Analyzing these results it has been demonstrated that the F₀ and F₁ parts of ATP synthases of these two bacteria are not functionally compatible.

【 授权许可】

Unknown