Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains
Department of Biochemistry and Molecular Pharmacology, Department of Neurobiology University of Massachusetts Medical School
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
Biochemistry | Biochemistry, Biophysics, and Structural Biology | Molecular Biology
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
J Biol Chem. 2005 Dec 9;280(49):40489-93. Epub 2005 Oct 10. Link to article on publisher's site
The Journal of biological chemistry
Karamyshev, Andrey L.; Kelleher, Daniel J.; Gilmore, Reid; Johnson, Arthur E.; von Heijne, Gunnar; and Nilsson, Ingmarie, "Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains" (2005). Biochemistry and Molecular Pharmacology Publications and Presentations. 183.