哺乳动物非经典分泌信号肽介导重组EGFP蛋白向毕赤酵母细胞壁转运

Delivery of recombinant enhanced green fluorescent protein to Pichia pastoris cell wall directed by a mammalian nonclassical secretion signal peptide

摘要:

为探索哺乳动物非经典分泌信号肽在毕赤酵母表达系统中引导重组蛋白分泌的作用，本研究将一段来源于小鼠同源异型框蛋白 (En2) 的分泌信号序列 (SS) 融合至EGFP蛋白的N端，在毕赤酵母中表达。实验结果显示SS信号肽能通过一种不同于经典的内质网-高尔基体分泌通路的方式将EGFP蛋白分泌至细胞膜表面，与α交配因子前导肽相比，显著降低了细胞的内质网压力。本研究提示哺乳动物非经典分泌信号肽可作为递送重组蛋白至酵母膜表面的一项工具。

Abstract:

A mammalian nonclassical secretion sequence derived from mouse Engrailed2 homeoprotein (En2) was used to direct the secretion of the enhanced green fluorescent protein from Pichia pastoris. This signal peptide conferred the transport of enhanced green fluorescent protein into periplasm through an endoplasmic reticulum-golgi independent pathway, without inducing severe unfolded protein response as compared with Saccharomyces cerevisae α-factor preprosequence. This study implies that this mammalian nonclassical signal peptide could be developed as a useful tool for delivering cargoes to the cell surface of yeast.