CHANNELS FORMED BY COLICIN-E1 IN PLANAR LIPID BILAYERS ARE LARGE AND EXHIBIT PH-DEPENDENT ION SELECTIVITY
CHANNELS FORMED BY COLICIN-E1 IN PLANAR LIPID BILAYERS ARE LARGE AND EXHIBIT PH-DEPENDENT ION SELECTIVITY
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DOI:
10.1007/bf01872215
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发表时间:
1985-01-01
影响因子:
2.4
通讯作者:
FINKELSTEIN, A
中科院分区:
文献类型:
--
作者:
RAYMOND, L;SLATIN, SL;FINKELSTEIN, A
The E1 subgroup (E1, A, Ib, etc.) of antibacterial toxins called colicins are known to form voltage-dependent channels in planar lipid bilayers. The genes for colicins E1, A and Ib have been cloned and sequenced, making these channels interesting models for the widespread phenomenon of voltage dependence in cellular channels. Ion selectivity and channel size.sbd.properties relevant to model building were investigated. Apparently, the colicin E1 channel is large, having a diameter of at least 8 A at its narrowest point. This was established from measurements of reversal potentials for gradients formed by salts of large cations or large anions. In so doing, the fact that the colicin channel is permeable to both cations and anions was exploited; its relative selectivity to them is a function of pH. The channel is anion selective (Cl over K+) in neutral membranes; the degree of selectivity is highly dependent on pH. In negatively charged membranes, it becomes cation selective at pH''s higher than about 5. Experiments with pH gradients cross the membrane suggest that titratable groups both within the channel lumen and near the channel ends affect the selectivity. Individual E1 channels have > 1 open conductance state, all displaying comparable ion selectivity. Colicins A and Ib also exhibit pH-dependent ion selectivity, and appear to have even larger lumens than E1.