Herscovics A, Orlean P
McGill Cancer Centre, McGill University, Montreal, Quebec, Canada.
FASEB J. 1993 Apr 1;7(6):540-50. doi: 10.1096/fasebj.7.6.8472892.
Many proteins in the yeast Saccharomyces cerevisiae are modified by the attachment of N-linked saccharides to asparagine, of O-linked mannose glycans to serine or threonine, and of glycosylphosphoinositol membrane anchors. The biosynthetic events leading to these modifications are coupled to the secretory pathway. Early stages of N-linked glycosylation and the formation of glycosylphosphoinositol anchors have been conserved through evolution of eukaryotes. Studies of yeast offer a variety of genetic and molecular biological approaches, which have led to the isolation of different glycosylation mutants and of genes for enzymes involved in glycosylation. Yeast mutants are useful to identify biosynthetic intermediates, to establish whether a given enzyme is essential for viability, and to determine how cellular functions are affected when glycosylation is perturbed. Yeast glycosylation mutants and genes can be used to identify their counterparts in other eukaryotes.
在酿酒酵母中，许多蛋白质会通过以下方式进行修饰：将N-连接寡糖连接到天冬酰胺上、将O-连接甘露糖聚糖连接到丝氨酸或苏氨酸上，以及连接糖基磷脂酰肌醇膜锚定物。导致这些修饰的生物合成过程与分泌途径相关联。N-连接糖基化的早期阶段以及糖基磷脂酰肌醇锚定物的形成在真核生物的进化过程中得以保留。对酵母的研究提供了多种遗传和分子生物学方法，这些方法已导致不同糖基化突变体以及参与糖基化的酶的基因的分离。酵母突变体有助于识别生物合成中间体，确定特定酶对于生存力是否必不可少，并确定糖基化受到干扰时细胞功能是如何受到影响的。酵母糖基化突变体和基因可用于识别其他真核生物中的对应物。
