CONFORMATIONS OF SIGNAL PEPTIDES INDUCED BY LIPIDS SUGGEST INITIAL STEPS IN PROTEIN EXPORT
CONFORMATIONS OF SIGNAL PEPTIDES INDUCED BY LIPIDS SUGGEST INITIAL STEPS IN PROTEIN EXPORT
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DOI：
10.1126/science.2941862
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发表时间：
1986-07-11
期刊：
影响因子：
56.9
通讯作者：
GIERASCH, LM
中科院分区：
文献类型：
--
作者：
BRIGGS, MS;CORNELL, DG;GIERASCH, LM
尽管在蛋白质出口的功能信号序列的要求，很少有人知道的构象特性和膜的相互作用，这些高度疏水性的氨基末端的延伸几乎所有的出口蛋白质。大肠埃希氏菌通过圆二色性和傅里叶变换红外光谱法在磷脂单层中研究噬菌体受体信号序列;显示信号肽偏好α-当插入到脂质相中时的螺旋构象。然而，在没有插入的情况下与脂质表面的相互作用诱导了在本体水溶液中非结构化的信号序列采用β。结构这些观察结果结合在一个模型中的信号序列在体内膜相互作用的初始步骤。
Despite the requirement for a functional signal sequence in protein export, little is known of the conformational properties and membrane interactions of these highly hydrophobic amino terminal extensions on nearly all exported proteins. The Escherichia coli .lambda. phage receptor signal sequence was studied in phospholipid monolayers by circular dichroism and Fourier transform infrared spectroscopy; the signal peptide was shown to prefer an .alpha.-helical conformation when inserted into the lipid phase. However, interaction with the lipid surface without insertion induced the signal sequence, which is unstructured in bulk aqueous solution, to adopt a .beta. structure. These observations are combined in a model for the initial steps in signal sequence-membrane interaction in vivo.