Yamamoto Y, Taniyama Y, Kikuchi M, Ikehara M
Protein Engineering Research Institute, Osaka Laboratory, Takeda Chemical Industries Ltd., Japan.
Biochem Biophys Res Commun. 1987 Dec 16;149(2):431-6. doi: 10.1016/0006-291x(87)90385-8.
To elucidate the structure-function relationship of the signal sequence for the secretion of human lysozyme by Saccharomyces cerevisiae, we have systematically engineered the hydrophobic segment using the signal sequence of chicken lysozyme. Replacement of Cys 10 with leucine caused a 1.6 times increase in the secretion of human lysozyme. An idealized signal sequence L10 in which 10 consecutive leucines were distributed from the 3rd to the 12th position was 1.8 times as effective as the native sequence. L10 can be generalized as Ln = Met-Arg-(Leu)n-Pro-Leu-Ala-Ala-Leu-Gly, where n = 10. We have also studied the secretory capability of Ln, where n = 6,8,12, and 14, and found that the length, as well as hydrophobicity, of the hydrophobic segment is an important factor in the secretion of human lysozyme by yeast.
为了阐明酿酒酵母分泌人溶菌酶的信号序列的结构-功能关系，我们利用鸡溶菌酶的信号序列对疏水片段进行了系统改造。将第10位的半胱氨酸替换为亮氨酸，使人溶菌酶的分泌增加了1.6倍。一种理想化的信号序列L10，其中从第3位到第12位分布着10个连续的亮氨酸，其效果是天然序列的1.8倍。L10可以概括为Ln = Met-Arg-(Leu)n-Pro-Leu-Ala-Ala-Leu-Gly，其中n = 10。我们还研究了n = 6、8、12和14时Ln的分泌能力，发现疏水片段的长度以及疏水性是酵母分泌人溶菌酶的一个重要因素。
