Inouye S, Duffaud G, Inouye M
J Biol Chem. 1986 Aug 25;261(24):10970-5.
A phenotypically silent mutation in the signal peptide of the Escherichia coli outer membrane prolipoprotein was combined with other mutations in the mature lipoprotein structure. Under conditions where the individual mutations permit normal lipoprotein secretion, the prolipoprotein with both mutations was unable to be normally modified or processed. These results demonstrate that a given signal peptide is fully functional only if it is structurally compatible with the protein to be secreted. This structural compatibility between the signal peptide and the secretory protein is considered to be dependent on the secondary structure formed at or near the signal peptide cleavage site.
大肠杆菌外膜前脂蛋白信号肽中的一个表型沉默突变与成熟脂蛋白结构中的其他突变相结合。在单个突变允许正常脂蛋白分泌的条件下，具有两种突变的前脂蛋白无法正常修饰或加工。这些结果表明，给定的信号肽只有在其结构与待分泌蛋白质相容时才具有完全功能。信号肽与分泌蛋白之间的这种结构相容性被认为取决于在信号肽切割位点或其附近形成的二级结构。
