INVIVO FUNCTION AND MEMBRANE-BINDING PROPERTIES ARE CORRELATED FOR ESCHERICHIA-COLI LAMB SIGNAL PEPTIDES
INVIVO FUNCTION AND MEMBRANE-BINDING PROPERTIES ARE CORRELATED FOR ESCHERICHIA-COLI LAMB SIGNAL PEPTIDES
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DOI：
10.1126/science.3158076
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发表时间：
1985-01-01
期刊：
影响因子：
56.9
通讯作者：
DEGRADO, WF
中科院分区：
文献类型：
--
作者：
BRIGGS, MS;GIERASCH, LM;DEGRADO, WF
对大肠杆菌lamB基因产物的野生型和假回复突变体信号肽进行了分析。大肠杆菌与脂质系统相互作用，而非功能性缺失突变信号肽则不与脂质系统相互作用。这一结论是基于合成的信号肽与脂质单层-水表面的相互作用，在信号肽的水溶液中的脂质囊泡的存在下诱导的构象变化和肽的促进囊泡聚集的能力。信号序列的分析和先前的构象研究表明，这些脂质相互作用性质可能归因于功能性信号肽采用α-螺旋构象虽然在蛋白质分泌过程中的信号肽和膜脂之间的直接相互作用的可能性是有争议的，结果表明，构象相关的两亲性和随之而来的膜亲和力的信号序列是重要的功能在体内。
Wild-type and pseudorevertant signal peptides of the lamB gene product of E. coli interact with lipid systems whereas a nonfunctional deletion mutant signal peptide does not. This conclusion is based on interaction of synthetic signal peptides with a lipid monolayer-water surface, conformational changes induced by presence of lipid vesicles in an aqueous solution of signal peptide and capacities of the peptides to promote vesicle aggregation. Analysis of the signal sequences and previous conformational studies suggest that these lipid interaction properties may be attributable to the tendency of the functional signal peptides to adopt .alpha.-helical conformations. Although the possibility of direct interaction between the signal peptide and membrane lipids during protein secretion is controversial, the results suggest that conformationally related amphiphilicity and consequent membrane affinity of signal sequences are important for function in vivo.