Burda P, Aebi M
Mikrobiologisches Institut, ETH Zürich, Schmelzbergstr. 7, CH-092 Zürich, Switzerland.
Biochim Biophys Acta. 1999 Jan 6;1426(2):239-57. doi: 10.1016/s0304-4165(98)00127-5.
The oligosaccharide substrate for the N-linked protein glycosylation is assembled at the membrane of the endoplasmic reticulum. Dolichyl pyrophosphate serves as a carrier in this biosynthetic pathway. In this review, we discuss the function of the lipid carrier dolichol in oligosaccharide assembly and give an overview of the biosynthesis of the different sugar donors required for the building of the oligosaccharide. Yeast genetic techniques have made it possible to identify many different loci encoding specific glycosyltransferases required for the precise and ordered assembly of the dolichyl pyrophosphate-linked oligosaccharide. Based on the knowledge obtained from studying this pathway in yeast, we compare it to the process of N-linked protein glycosylation in archaea. We suggest that N-linked glycosylation in eukaryotes and in archaea share a common evolutionary origin.
用于 N 连接蛋白糖基化的寡糖底物在内质网的膜上组装。焦磷酸多萜醇在这条生物合成途径中充当载体。在本综述中，我们讨论了脂质载体多萜醇在寡糖组装中的功能，并概述了构建寡糖所需的不同糖供体的生物合成。酵母遗传技术使得鉴定许多不同的基因座成为可能，这些基因座编码焦磷酸多萜醇连接的寡糖精确且有序组装所需的特定糖基转移酶。基于从酵母中研究这条途径所获得的知识，我们将其与古细菌中 N 连接蛋白糖基化的过程进行比较。我们认为真核生物和古细菌中的 N 连接糖基化具有共同的进化起源。
