Title

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

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology, Department of Neurobiology University of Massachusetts Medical School

Publication Date

2005-12-09

Document Type

Article

Subjects

Animals; Binding Sites; Cattle; Cross-Linking Reagents; Glycosylation; Hexosyltransferases; Light; Membrane Proteins; Mutagenesis, Site-Directed; Peptides; Polysaccharides; Prolactin; Protein Precursors; RNA, Messenger; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship

Disciplines

Biochemistry | Biochemistry, Biophysics, and Structural Biology | Molecular Biology

Abstract

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 approximately 15 residues surrounding a QK(*)T cross-linking site impairs the interaction between the nascent chain and STT3.

DOI of Published Version

10.1074/jbc.M509168200

Source

J Biol Chem. 2005 Dec 9;280(49):40489-93. Epub 2005 Oct 10. Link to article on publisher's site

Journal/Book/Conference Title

The Journal of biological chemistry

Related Resources

Link to Article in PubMed

PubMed ID

16216884

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