Gooley A A, Classon B J, Marschalek R, Williams K L
School of Biological Sciences, Macquarie University, Sydney, N.S.W. Australia.
Biochem Biophys Res Commun. 1991 Aug 15;178(3):1194-201. doi: 10.1016/0006-291x(91)91019-9.
Here we report the use of automated Edman degradation of covalently linked glycopeptides to identify positively the sites of O- and N-glycosylation. The O-glycosidic linkage of carbohydrate to the hydroxy amino acids Ser and Thr is a major form of post-translational modification. However, unlike Asn-linked glycosylation, which is identified by the consensus sequence Asn-Xaa-Thr/Ser, no simple motif conferring O-linkage to Thr and Ser has been described. After sequencing glycopeptides derived from two cell surface glycoproteins, a Thr-O-glycosylation motif of Xaa-Pro-Xaa-Xaa, where at least one Xaa = Thr(Sac), has been defined. This motif predicts the site(s) of Pro- associated Thr-O-glycosylation in O-glycosylated proteins, although it is clear that there are also other forms of Thr-O-glycosylation not associated with Pro.
在此，我们报告了利用共价连接的糖肽的自动埃德曼降解法来明确鉴定O-糖基化和N-糖基化位点。碳水化合物与羟基氨基酸丝氨酸（Ser）和苏氨酸（Thr）的O-糖苷键连接是一种主要的翻译后修饰形式。然而，与通过共有序列Asn-Xaa-Thr/Ser鉴定的天冬酰胺连接的糖基化不同，尚未描述赋予Thr和Ser O-连接的简单基序。在对源自两种细胞表面糖蛋白的糖肽进行测序后，定义了一个Xaa-Pro-Xaa-Xaa的苏氨酸-O-糖基化基序，其中至少有一个Xaa = Thr（Sac）。该基序可预测O-糖基化蛋白中与脯氨酸相关的苏氨酸-O-糖基化位点，尽管很明显还存在其他与脯氨酸无关的苏氨酸-O-糖基化形式。
