F0 and F1 parts of ATP synthases from Clostridium thermoautotrophicum and Escherichia coli are not functionally compatible.
F1-stripped membrane vesicles from Clostridium thermoautotrophicum and Escherichia coli were reconstituted with F1-ATPases from both bacteria. Reconstituted F1F0-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 of anilinonaphthalene 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.
Das
A
A
Center for Biological Resource Recovery, University of Georgia, Athens 30602.
Ljungdahl
L G
LG
D000255:Adenosine Triphosphate / Q000378:metabolism; D001667:Binding, Competitive; D003013:Clostridium / Q000201:enzymology*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D008565:Membrane Proteins; D004024:Dicyclohexylcarbodiimide; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases