HEESEN, ST and JANETZKY, B and LEHLE, L and AEBI, M (1992) THE YEAST WBP1 IS ESSENTIAL FOR OLIGOSACCHARYL TRANSFERASE-ACTIVITY INVIVO AND INVITRO. EMBO JOURNAL, 11 (6). pp. 2071-2075. ISSN 0261-4189, 1460-2075
Full text not available from this repository.Abstract
Asparagine-linked N-glycosylation is a highly conserved and functionally important modification of proteins in eukaryotic cells. The central step in this process is a cotranslational transfer of lipid-linked core oligosaccharides to selected Asn-X-Ser/Thr-sequences of nascent polypeptide chains, catalysed by the enzyme N-oligosaccharyl transferase. In this report we show that the essential yeast protein WBP1 (te Heesen et al., 1991) is required for N-oligosaccharyl transferase in vivo and in vitro. Depletion of WBP1 correlates with a defect in transferring core oligosaccharides to carboxypeptidase Y and proteinase A in vivo. In addition, in vitro N-glycosylation of the acceptor peptide Tyr-Asn-Leu-Thr-Ser-Val using microsomal membranes from WBP1 depleted cells is reduced as compared with membranes from wild-type cells. We propose that WBP1 is an essential component of the oligosaccharyl transferase in yeast.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SACCHAROMYCES-CEREVISIAE; PROTEIN GLYCOSYLATION; CARBOXYPEPTIDASE-Y; MUTANTS DEFICIENT; N-GLYCOSYLATION; GENE; PATHWAY; VACUOLE; ENDOPLASMIC RETICULUM; GLYCOSYLATION; OLIGOSACCHARYL TRANSFERASE; SACCHAROMYCES-CEREVISIAE; TRANSMEMBRANE PROTEIN |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54508 |
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