Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains

被引：20

作者：

Karamyshev, AL

Kelleher, DJ

Gilmore, R

Johnson, AE

von Heijne, G

Nilsson, I ^{[1
]}

机构：

[1] Stockholm Univ, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden

[2] Texas A&M Univ, Syst Hlth Sci Ctr, Dept Med Biochem & Genet, College Stn, TX 77843 USA

[3] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA

[4] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA

[5] Univ Massachusetts, Sch Med, Dept Mol Pharmacol & Biochem, Worcester, MA 01655 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2005年 / 280卷 / 49期

关键词：

D O I：

10.1074/jbc.M509168200

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：

Many secretory and membrane proteins are N-glycosylated by the oligosaccharyl transferase complex during their translocation across the endoplasmic reticulum membrane. Several experimental observations suggest that the highly conserved STT3 subunit contains the active site of the oligosaccharyl transferase. Here, we report a detailed study of the interaction between the active site of the STT3 protein and nascent polypeptide chains using an in vitro photocrosslinking technique. Our results show that the addition of a glycan moiety in a stretch of similar to 15 residues surrounding a QK*T cross-linking site impairs the interaction between the nascent chain and STT3.

引用

收藏

页码：40489 / 40493

页数：5

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