AMINO-ACID DISTRIBUTIONS AROUND O-LINKED GLYCOSYLATION SITES

被引:255
作者
WILSON, IBH
GAVEL, Y
VONHEIJNE, G
机构
[1] ROYAL INST TECHNOL,DEPT THEORET PHYS,THEORET BIOPHYS RES GRP,S-10044 STOCKHOLM 70,SWEDEN
[2] KAROLINSKA INST,CTR BIOTECHNOL,NOVUM,DEPT MOLEC BIOL,S-14152 HUDDINGE,SWEDEN
关键词
D O I
10.1042/bj2750529
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:529 / 534
页数:6
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