title: Structural and functional relationship of ATP synthases (F1F0) from Escherichia coli and the thermophilic bacterium PS3.
abstract: Functional compatibility between the F1 and F0 parts of ATP synthases from Escherichia coli (EF1F0) and the thermophilic bacterium PS3 (TF1F0) was analyzed. F1-stripped everted membrane vesicles from both organisms bound the homologous or heterologous F1 part to the same extent. Titration of the reconstituted membrane vesicles with dicyclohexylcarbodiimide revealed a similar sensitivity of the homologous and hybrid F1F0 complexes towards the inhibitor. Furthermore, the heterologous enzymes exhibited ATP-dependent H+ translocation comparable to that of homologous F1F0. Antisera raised against EF1 or subunits a, b, and c of EF0 were analyzed for cross-reactivity with TF1 and TF0. Common antigenic sites have been detected with immunoblot analysis for subunit beta and subunit c of EF1F0 and the corresponding subunits from TF1F0. A weak binding of the anti-a and anti-b antisera with the TF0 part has been observed in an enzyme-linked immunosorbent assay. Based on these findings the structural and functional relationship between the mesophilic and thermophilic ATP synthase complexes is discussed.
mesh_terms: D003429:Cross Reactions; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D000939:Epitopes / Q000032:analysis; D004926:Escherichia coli / Q000201:enzymology*; D007106:Immune Sera; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D000939:Epitopes; D007106:Immune Sera; D004024:Dicyclohexylcarbodiimide; D006180:Proton-Translocating ATPases