Steffens K, Di Gioia A, Deckers-Hebestreit G, Altendorf K
J Biol Chem. 1987 May 5;262(13):6334-8.
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.
分析了来自大肠杆菌（EF1F0）和嗜热细菌PS3（TF1F0）的ATP合酶F1和F0部分之间的功能兼容性。两种生物体去除F1的外翻膜囊泡对同源或异源F1部分的结合程度相同。用二环己基碳二亚胺滴定重组膜囊泡表明，同源和杂合F1F0复合物对该抑制剂的敏感性相似。此外，异源酶表现出与同源F1F0相当的ATP依赖性H+转运。分析了针对EF1或EF0的亚基a、b和c产生的抗血清与TF1和TF0的交叉反应性。通过免疫印迹分析检测到EF1F0的β亚基和c亚基以及TF1F0的相应亚基存在共同抗原位点。在酶联免疫吸附测定中观察到抗a和抗b抗血清与TF0部分有弱结合。基于这些发现，讨论了嗜温与嗜热ATP合酶复合物之间的结构和功能关系。
