Meyer R K, Schindler H, Burger M M
Proc Natl Acad Sci U S A. 1982 Jul;79(14):4280-4. doi: 10.1073/pnas.79.14.4280.
A method was developed to identify specific protein-lipid interactions of complex lipid mixtures and to assess their effect upon the arrangement of such complexes in monolayers at an air-water interface. Its application to striated muscle alpha-actinin revealed that just two lipids selectively interact with alpha-actinin. One molecule of glyceride and one molecule of fatty acid were found to be associated in a constant stoichiometry with one molecule of the alpha-actinin dimer. In the presence of both glycerides and fatty acids unexpectedly rigid monolayer areas formed. This lipid specificity could be confirmed by brief protease digestion of alpha-actinin liposome mixtures followed by peptide analysis; the peptide patterns of alpha-actinin depended on the presence or absence of only these two lipids. Possible implications of these findings are discussed in the context of Z-line formation.
开发了一种方法,用于识别复杂脂质混合物中特定的蛋白质 - 脂质相互作用,并评估它们对这种复合物在空气 - 水界面单层中的排列的影响。将其应用于横纹肌α - 肌动蛋白时发现,只有两种脂质与α - 肌动蛋白选择性相互作用。发现一分子甘油酯和一分子脂肪酸以恒定的化学计量与一分子α - 肌动蛋白二聚体结合。在甘油酯和脂肪酸同时存在的情况下,意外地形成了刚性单层区域。通过对α - 肌动蛋白脂质体混合物进行短暂的蛋白酶消化,然后进行肽分析,可以证实这种脂质特异性;α - 肌动蛋白的肽图谱仅取决于这两种脂质的存在与否。在Z线形成的背景下讨论了这些发现的可能意义。