KNAUER, R and LEHLE, L (1994) THE N-OLIGOSACCHARYLTRANSFERASE COMPLEX FROM YEAST. FEBS LETTERS, 344 (1). pp. 83-86. ISSN 1873-3468,
Full text not available from this repository.Abstract
N-Oligosaccharyltransferase catalyzes the N-glycosylation of asparagine residues of nascent polypeptide chains in the endoplasmic reticulum, a pathway highly conserved in all eukaryotes. An enzymatically active complex was isolated from microsomal membranes from Saccharomyces cerevisiae, which is composed of four proteins: Wbp1p and Swp1p (previously found to be encoded by two essential genes necessary for N-glycosylation in vivo and in vitro) and two additional proteins with a molecular mass of 60/62 kDa and 34 kDa. The 60/62 component represents differentially glycosylated forms of a protein that has sequence homology to ribophorin I. Wbp1p and Swp1p reveal homology to mammalian OST 48 and ribophorin II, respectively. Ribophorin I and II and OST 48 were recently shown to be constituents of the mammalian transferase from dog pancreas. The data reveal a high conservation of the organization of this enzyme activity.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ROUGH ENDOPLASMIC-RETICULUM; RIBOPHORIN-II; PROTEINS; GLYCOSYLATION; GLYCOPROTEIN; PURIFICATION; TRANSFERASE; OLIGOSACCHARYLTRANSFERASE; PROTEIN GLYCOSYLATION; GLYCOPROTEIN; ENDOPLASMIC RETICULUM; DOLICHOL; SACCHAROMYCES CEREVISIAE |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53282 |
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