Relations between structure and function in cytoplasmic membrane vesicles isolated from an Escherichia coli fatty-acid auxotroph. High-angle x-ray diffraction, freeze-etch electron microscopy and transport studies.
Relations between structure and function in cytoplasmic membrane vesicles isolated from an Escherichia coli fatty-acid auxotroph. High-angle x-ray diffraction, freeze-etch electron microscopy and transport studies.
复制标题
从大肠杆菌脂肪酸营养缺陷型分离的细胞质膜囊泡的结构和功能之间的关系。
DOI:
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发表时间:
1974
期刊:
影响因子:
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通讯作者:
T. Gulik
中科院分区:
文献类型:
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作者:
E. Shechter;L. Letellier;T. Gulik
The results presented in this paper establish relationships between structural, morphological and functional properties of cytoplasmic membrane vesicles isolated from an Escherichia coli unsaturated fatty acid auxotroph. The membranes were isolated from cells grown in the presence of either oleic, linoleic, linolenic or elaidic acids.
High-angle X-ray diffraction studies show that the order-disorder transitions induced by temperature variations and associated with the paraffin chains of the lipids are a function of the fatty acid composition of the membranes. In some cases “cocrystallization” of various lipid species takes place within a single type of ordered domains. In other cases there is segregation of various lipid species into more than one distinct type of ordered domain.
The various order-disorder transitions observed induce morphological changes in the hydrophobic core of the membranes which can be detected by freeze-etch electron microscopy. A random distribution of particles on the fracture faces is observed when the paraffin chains of the lipids are disordered. Upon ordering of the paraffin chains, particles are excluded from the ordered domains and as a consequence, smooth areas and areas with densely packed particles are observed. The ratio of the smooth surface to particulated surface is proportional to the amount of ordered paraffin chains present. Moreover, the size of the smooth domains is a function of the fatty acid composition of the membranes.
Discontinuities in the rate of d-lactate-dependent proline uptake as a function of temperature correlate with the order-disorder transitions observed. The high energies of activation at low temperatures are attributed to decreased mobility of the carrier proteins upon aggregation. In contrast, phosphoenolpyruvate-dependent vectorial phosphorylation does not respond to the ordering of the paraffin chains.