Braspenning J, Meschede W, Marchini A, Müller M, Gissmann L, Tommasino M
Deutsches Krebsforschungszentrum, Angewandte Tumorvirologie, INF, 242, 69120 Heidelberg, Germany.
Biochem Biophys Res Commun. 1998 Apr 7;245(1):166-71. doi: 10.1006/bbrc.1998.8402.
In this study we report the use of the S. pombe leader sequence of pho1+ acid phosphatase (Elliott et al., J. Biol. Chem. 216, 2916-2941, 1986) for the secretion of heterologous proteins into the medium. The green fluorescent protein (GFP) and the Human Papillomavirus (HPV) type 16 E7 protein are normally not secreted; fusion of the S. pombe pho1 leader peptide (SPL) to GFP and HPV 16 E7 resulted in an efficient secretion of these proteins although the latter contains a nuclear targeting sequence. These data suggest that SPL fused constructs could be applied for the production of other recombinant proteins using the S. pombe expression system. Furthermore, since GFP retains its intrinsic fluorescence during the secretion, this system may be useful to study the secretory pathway of fission yeast in vivo.
在本研究中，我们报道了利用粟酒裂殖酵母酸性磷酸酶pho1⁺（Elliott等人，《生物化学杂志》216, 2916 - 2941, 1986）的前导序列将异源蛋白分泌到培养基中。绿色荧光蛋白（GFP）和人乳头瘤病毒16型（HPV-16）E7蛋白通常不会被分泌；将粟酒裂殖酵母pho1前导肽（SPL）与GFP和HPV-16 E7融合，导致这些蛋白有效分泌，尽管后者含有一个核定位序列。这些数据表明，融合SPL的构建体可用于利用粟酒裂殖酵母表达系统生产其他重组蛋白。此外，由于GFP在分泌过程中保留其固有荧光，该系统可能有助于在体内研究裂殖酵母的分泌途径。
