F0 and F1 parts of ATP synthases from Clostridium thermoautotrophicum and Escherichia coli are not functionally compatible
- 8 February 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 317 (1-2) , 17-21
- https://doi.org/10.1016/0014-5793(93)81482-f
Abstract
F1-stripped membrane vesicles from Clostridium thermoautotrophicum and Escherichia coli were reconstituted with F1-ATPases from both bacteria. Reconstituted FiFo-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.Keywords
This publication has 24 references indexed in Scilit:
- ATP SYNTHASE (H+-ATPase): Results by Combined Biochemical and Molecular Biological ApproachesAnnual Review of Biochemistry, 1989
- The Autotrophic Pathway of Acetate Synthesis in Acetogenic BacteriaAnnual Review of Microbiology, 1986
- Reconstitution of photophosphorylation with coupling factor 1 ATPases from the thermophilic bacterium PS3 and lettuce chloroplastsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1985
- Comparison of F1's of oxidative phosphorylation from Escherichia coli and Salmonella typhimurium and demonstration of interchangeability of their subunitsBiochemistry, 1984
- Clostridium thermoautotrophicum species novum, a thermophile producing acetate from molecular hydrogen and carbon dioxideCurrent Microbiology, 1981
- The Mechanism and Regulation of ATP Synthesis by F1-ATPasesAnnual Review of Biochemistry, 1981
- The Proton‐Translocating Adenosine Triphosphatase of the Obligately Anaerobic Bacterium Clostridium pusteuriunumEuropean Journal of Biochemistry, 1979
- A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samplesAnalytical Biochemistry, 1978
- Electrochemical potential of protons in vesicles reconstituted from purified, proton-translocating adenosine triphosphataseThe Journal of Membrane Biology, 1976
- Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfateAnalytical Biochemistry, 1971