HEESEN, ST and KNAUER, R and LEHLE, L and AEBI, M (1993) YEAST WBP1P AND SWP1P FORM A PROTEIN COMPLEX ESSENTIAL FOR OLIGOSACCHARYL TRANSFERASE-ACTIVITY. EMBO JOURNAL, 12 (1). pp. 279-284. ISSN 0261-4189, 1460-2075
Full text not available from this repository.Abstract
Asparagine-linked N-glycosylation is an essential protein modification occurring in all eukaryotic cells. The central step is the co-translational transfer of the core oligosaccharide assembled on the lipid carrier dolichol phosphate to selected Asn-X-Ser/Thr residues of nascent polypeptide chains in the endoplasmic reticulum. This reaction is catalyzed by the enzyme N-oligosaccharyl transferase. In yeast, Wbp1p is an essential component of this enzyme. Using a high copy number suppression approach, the SWP1 gene was isolated as an allele specific suppressor of a wbp1 mutation. Swp1p is a 30 kDa type I transmembrane protein and essential for cell viability. Similar to Wbp1p, depletion of Swp1p results in reduced N-oligosaccharyl transferase activity in vivo and in vitro. Wbp1p and Swp1p can be chemically cross-linked, suggesting that both proteins are essential constituents of the N-oligosaccharyl transferase complex.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ROUGH ENDOPLASMIC-RETICULUM; SACCHAROMYCES-CEREVISIAE; CARBOXYPEPTIDASE-Y; ESCHERICHIA-COLI; SHUTTLE VECTORS; RIBOPHORIN-I; MEMBRANE; GLYCOSYLATION; EXPRESSION; TRANSPORT; ENDOPLASMIC RETICULUM; GLYCOSYLATION; OLIGOSACCHARYL TRANSFERASE; SACCHAROMYCES-CEREVISIAE; TRANSMEMBRANE PROTEIN |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:43 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54179 |
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