Role of the delta subunit in enhancing proton conduction through the F0 of the Escherichia coli F1F0 ATPase.
Role of the delta subunit in enhancing proton conduction through the F0 of the Escherichia coli F1F0 ATPase.
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δ 亚基通过大肠杆菌 F1F0 ATP 酶的 F0 增强质子传导的作用。
DOI：
10.1128/jb.176.5.1383-1389.1994
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发表时间：
1994
影响因子：
3.2
通讯作者：
Brusilow,WS
中科院分区：
文献类型：
--
作者：
Monticello,RA;Brusilow,WS
我们研究了大肠杆菌F1 atp酶的δ亚基对体内合成和组装的F0质子通道质子通透性的影响。从携带含有F0亚基和δ亚基基因的质粒的unc缺失菌株分离的膜对质子的渗透性明显高于从携带仅含有F0亚基基因的质粒的同一菌株分离的膜。这种增加的质子渗透性可以通过二环己基碳二亚胺或纯化F1处理来阻断，两者都可以阻断质子通过F0的传导。在体外用纯化的F1重组后，两种膜制剂都能将质子泵送耦合到ATP水解。这些结果表明，在合成和组装过程中，δ亚基与F0之间的相互作用使F0质子通道的质子渗透率发生了显著变化。
We studied the effect of the delta subunit of the Escherichia coli F1 ATPase on the proton permeability of the F0 proton channel synthesized and assembled in vivo. Membranes isolated from an unc deletion strain carrying a plasmid containing the genes for the F0 subunits and the delta subunit were significantly more permeable to protons than membranes isolated from the same strain carrying a plasmid containing the genes for the F0 subunits alone. This increased proton permeability could be blocked by treatment with either dicyclohexyl-carbodiimide or purified F1, both of which block proton conduction through the F0. After reconstitution with purified F1 in vitro, both membrane preparations could couple proton pumping to ATP hydrolysis. These results demonstrate that an interaction between the delta subunit and the F0 during synthesis and assembly produces a significant change in the proton permeability of the F0 proton channel.