A biophysical study of protein-lipid interactions in membranes of Escherichia coli. Fluoromyristic acid as a probe.
A biophysical study of protein-lipid interactions in membranes of Escherichia coli. Fluoromyristic acid as a probe.
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大肠杆菌膜中蛋白质-脂质相互作用的生物物理学研究。
DOI：
10.1016/s0006-3495(81)84882-5
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发表时间：
1981
影响因子：
3.4
通讯作者：
Ho,C
中科院分区：
文献类型：
--
作者：
Gent,MP;Cottam,PF;Ho,C
本文用~（19）F核磁共振波谱和转运分析研究了大肠杆菌K1060 B5和ML 308-225-乌法-8两株不饱和脂肪酸营养缺陷型细胞的膜性质。肉豆蔻酸的氟化类似物8，8-二氟肉豆蔻酸可通过取代生长培养基中的油酸酯而掺入膜磷脂中。在8，8-二氟肉豆蔻酸盐上生长一代导致膜中氟化脂肪酸的含量为20%，蛋白质与脂质比率的变化，以及甲基β-D-硫代半乳糖苷的转运改变。结果表明，油酸对E.大肠杆菌K1060 B5相对于ML 308-225-乌法-8的转化率通过掺入8，8-二氟肉豆蔻酸酯而增强。相变行为变得明显不同，并且在转变温度以上的脂质组织中存在一些差异。与此同时，甲基β-D-硫代半乳糖苷的浓度速率和程度在大肠杆菌中降低了两倍以上。大肠杆菌K1060 B5与ML 308-225-乌法-8相比。这种行为表明，这些氟化脂肪酸补充菌株的E。大肠杆菌中的蛋白质是有用的，以研究蛋白质-脂质相互作用的细微差异和它们对膜结合酶的功能的影响。
Fluorine-19 nuclear magentic resonance spectroscopy and transport assays have been used to investigate and compare the membrane properties of unsaturated fatty acid auxotrophs of two strains of Escherichia coli, K1060B5 and ML 308–225-UFA-8. A fluorinated analog of myristic acid, 8, 8-difluoromyristic acid, can be incorporated into the membrane phospholipids by substitution for oleate in the growth medium. Growth for one generation on 8, 8-difluoromyristate results in a 20% content of fluorinated fatty acid in the membranes, changes in the protein to lipid ratio, and altered transport of methyl beta-D-thiogalactopyranoside. The differences in membrane composition and transport behavior seen in oleate supplemented E. coli K1060B5 relative to ML 308–225-UFA-8 are enhanced by the incorporation of 8, 8-difluoromyristate. The phase transition behavior becomes distinctly different and some differences in lipid organization persist above the transition temperature. Concomitantly, the rate and extent of concentration of methyl beta-D-thiogalactopyranoside are reduced two-fold more in E. coli K1060B5 compared to ML 308–225-UFA-8. Such behavior suggests that these fluorinated fatty acid supplemented strains of E. coli are useful to study subtle differences in protein-lipid interactions and their effects on the function of membrane-bound enzymes.