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

Andrey L. Karamyshev, Daniel J. Kelleher, Reid Gilmore, Arthur E. Johnson, Gunnar Von Heijne, Ingmarie Nilsson

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19 Scopus citations

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

Original languageEnglish (US)
Pages (from-to)40489-40493
Number of pages5
JournalJournal of Biological Chemistry
Volume280
Issue number49
DOIs
Publication statusPublished - Dec 9 2005

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Karamyshev, A. L., Kelleher, D. J., Gilmore, R., Johnson, A. E., Von Heijne, G., & Nilsson, I. (2005). Mapping the interaction of the STT3 subunit of the oligosaccharyl transferase complex with nascent polypeptide chains. Journal of Biological Chemistry, 280(49), 40489-40493. https://doi.org/10.1074/jbc.M509168200