Kumamoto C A, Simoni R D
J Biol Chem. 1986 Aug 5;261(22):10037-42.
A mutation of the b subunit of the Escherichia coli proton translocating ATPase was previously described (Porter, A. C. G., Kumamoto, C., Aldape, K., and Simoni, R. D. (1985) J. Biol. Chem. 260, 8182-8187). This mutation, which causes substitution of aspartic acid for glycine at position 9 (basp9), results in loss of function of the ATPase complex. In this paper we describe the isolation and characterization of two mutations that partially suppress the effects of the basp9 alteration. The suppressor mutations cause amino acid substitutions at position 240 of the a subunit. Membranes derived from strains carrying a suppressor mutation and the basp9 mutation exhibited ATP-dependent proton translocating activity.
先前曾描述过大肠杆菌质子转运ATP酶β亚基的一种突变（波特，A.C.G.，熊本，C.，阿尔达佩，K.，和西蒙尼，R.D.（1985年）《生物化学杂志》260，8182 - 8187）。这种突变导致第9位的甘氨酸被天冬氨酸替代（β asp9），致使ATP酶复合体功能丧失。在本文中，我们描述了两个部分抑制β asp9改变效应的突变的分离和特性。这些抑制突变导致α亚基第240位的氨基酸替代。携带抑制突变和β asp9突变的菌株来源的膜表现出ATP依赖的质子转运活性。
