AMINO-ACID DISTRIBUTIONS AROUND O-LINKED GLYCOSYLATION SITES
AMINO-ACID DISTRIBUTIONS AROUND O-LINKED GLYCOSYLATION SITES
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DOI：
10.1042/bj2750529
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发表时间：
1991-04-15
影响因子：
4.1
通讯作者：
VONHEIJNE, G
中科院分区：
文献类型：
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作者：
WILSON, IBH;GAVEL, Y;VONHEIJNE, G
为了研究向蛋白质中添加O-连接的N-乙酰半乳糖胺的序列要求，将174个O-糖基化位点周围的氨基酸分布与非糖基化位点周围的分布进行比较。 与非糖基化的丝氨酸和苏氨酸残基相比，O-糖基化位点附近最突出的特征是脯氨酸残基的频率显著增加，尤其是在相对于糖基化残基的位置-1和+3处。 丙氨酸、丝氨酸和苏氨酸也显著增加。 O-糖基化区域的高丝氨酸和苏氨酸含量是由于在许多O-糖基化蛋白质中存在几个紧密间隔的糖基化羟基氨基酸的簇。 在某些情况下，可以从一级序列预测这样的簇，但是从一级序列数据预测分离的O-糖基化位点没有明显的可能性。
To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data.