Friedl P, Hoppe J, Gunsalus R P, Michelsen O, von Meyenburg K, Schairer H U
Department of Stoffwechselregulation, GBF-Gesellschaft für Biotechnologische Forschung mbH., Braunschweig-Stöckheim, FRG.
EMBO J. 1983;2(1):99-103. doi: 10.1002/j.1460-2075.1983.tb01388.x.
Integration into the cytoplasmic membrane and function of the three F0 subunits, a, b and c, of the membrane-bound ATP synthase of Escherichia coli K12 were analysed in situations where synthesis of only one or two types of subunits was possible. This was achieved by combined use of atp mutations and plasmids carrying and expressing one or two of the atp genes coding for ATP synthase subunits. AU three F0 subunits were found to be required for the establishment of efficient H+ conduction. Subunits a and b individually as well as together were found to bind F1 ATPase to the membrane while subunit c did not. The ATPase activity bound to either of these single subunits, or in pairwise combinations, was not inhibited by N,N'-dicyclohexylcarbodiimide. Also ATP-dependent H+ translocation was not catalysed unless all three F0 subunits were present in the membrane. The integration into the membrane of the subunits a and b was independent of the presence of other ATP synthase subunits.
在仅能合成一种或两种类型亚基的情况下，对大肠杆菌K12膜结合型ATP合酶的三个F0亚基a、b和c整合到细胞质膜及其功能进行了分析。这是通过联合使用atp突变体和携带并表达编码ATP合酶亚基的一个或两个atp基因的质粒来实现的。发现所有三个F0亚基都是建立高效H+传导所必需的。发现亚基a和b单独以及一起都能将F1 ATP酶结合到膜上，而亚基c则不能。与这些单个亚基中的任何一个结合或以成对组合形式结合的ATP酶活性不受N，N'-二环己基碳二亚胺抑制。而且，除非膜中存在所有三个F0亚基，否则不会催化ATP依赖性H+转运。亚基a和b整合到膜中与其他ATP合酶亚基的存在无关。
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