Scotti P A, Praestegaard M, Chambert R, Petit-Glatron M F
Institut Jacques Monod, CNRS, Université Paris 7, France.
Yeast. 1996 Aug;12(10):953-63. doi: 10.1002/(SICI)1097-0061(199608)12:10%3C953::AID-YEA998%3E3.0.CO;2-#.
We compared the ability of signal sequences from various Bacillus or yeast secreted proteins to direct Bacillus subtilis levansucrase into the secretion pathway of the yeast Saccharomyces cerevisiae. The efficiency of these sequences correlated with the overall hydrophobicity of their h-domain and was independent of their origin. Furthermore, the net charge of the proximal protein sequence downstream from the signal sequence contributed to the competence of the heterologous proteins to be secreted by yeast. Modification of this net charge allowed the protein to be translocated under the control of the yeast invertase signal sequence. Moreover, glycosylation of levansucrase did not modify significantly the fructosyl polymerase activity.
我们比较了来自各种芽孢杆菌或酵母分泌蛋白的信号序列将枯草芽孢杆菌果聚糖蔗糖酶导入酿酒酵母分泌途径的能力。这些序列的效率与其h结构域的整体疏水性相关，且与其来源无关。此外，信号序列下游近端蛋白质序列的净电荷有助于异源蛋白被酵母分泌的能力。对该净电荷的修饰使得蛋白质能够在酵母转化酶信号序列的控制下进行转运。此外，果聚糖蔗糖酶的糖基化并未显著改变果糖基聚合酶活性。
