一种由大肠杆菌的F1和嗜盐栖热菌的F0组成的杂合腺苷三磷酸酶是一种功能性钠离子泵。
A hybrid adenosinetriphosphatase composed of F1 of Escherichia coli and F0 of Propionigenium modestum is a functional sodium ion pump.
作者信息
Laubinger W, Deckers-Hebestreit G, Altendorf K, Dimroth P
机构信息
Institut für Physiologische Chemie, Technischen Universität München, FRG.
出版信息
Biochemistry. 1990 Jun 12;29(23):5458-63. doi: 10.1021/bi00475a008.
Analyses on immunoblots indicated strong binding of the alpha- and beta-subunits of the ATPase of Propionigenium modestum to antibodies raised against the corresponding subunits of the F1F0 ATPase of Escherichia coli. Cross-reactivities of antibodies against the other ATPase subunits were not observed. The use of Na+ or H+ as alternate coupling ions, observed previously for the P. modestum ATPase [Laubinger, W., & Dimroth, P. (1989) Biochemistry 28, 7194-7198], is not found for the F1F0 ATPase of E. coli, which is specific for protons. However, a hybrid consisting of the F1 moiety of the E. coli ATPase and F0 of that from P. modestum performed Na+ or H+ transport in a reconstituted system. As with the homologous ATPase of P. modestum, H+ pumping of the hybrid was abolished at Na+ concentrations of greater than 1 mM. The F0 sector and not F1, therefore, determines the cation specificity of these F1F0 ATPases.
免疫印迹分析表明，嗜盐栖丙酸杆菌ATP酶的α亚基和β亚基与针对大肠杆菌F1F0 ATP酶相应亚基产生的抗体有强烈结合。未观察到针对其他ATP酶亚基的抗体的交叉反应性。嗜盐栖丙酸杆菌ATP酶先前观察到使用Na⁺或H⁺作为交替偶联离子[劳宾格，W.，& 迪姆罗思，P.（1989年）《生物化学》28，7194 - 7198]，而大肠杆菌的F1F0 ATP酶对质子具有特异性，未发现这种情况。然而，由大肠杆菌ATP酶的F1部分和嗜盐栖丙酸杆菌的F0组成的杂种在重构系统中进行Na⁺或H⁺转运。与嗜盐栖丙酸杆菌的同源ATP酶一样，当Na⁺浓度大于1 mM时，杂种的H⁺泵浦作用被消除。因此，是F0部分而非F1部分决定了这些F1F0 ATP酶的阳离子特异性。
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