Schwarz, Markus and Knauer, Roland and Lehle, Ludwig (2005) Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit. FEBS LETTERS, 579 (29). pp. 6564-6568. ISSN 1873-3468,
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The key step of N-glycosylation of proteins in the endoplasmic reticulum is catalyzed by the hetero-oligomeric protein complex oligosaccharyltransferase (OST). It transfers the lipid-linked core-oligosaccharide to selected Asn-X-Ser/Thrsequences of nascent polypeptide chains. Biochemical and genetic approaches have revealed that OST from Saccharomyces cerevisiae consists of nine subunits: Wbp1p, Swp1p, Stt3p, Ost1p, Ost2p, Ost4p, Ost5p, Ostp3 and Ost6p. By blue native polyacrylamide electrophoresis we show that yeast OST consists of two isoforms with distinct functions differing only in the presence of the two related Ost3 and Ost6p proteins. The OST6-complex was found to be important for cell wall integrity and temperature stress. Ost3p and Ost6p are not essential for OST activity, and can in part displace each other in the complex when overexpressed, suggesting a dynamic regulation of the complex formation. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BLUE NATIVE ELECTROPHORESIS; MEMBRANE-PROTEIN COMPLEXES; ACTIVITY IN-VIVO; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM; STT3 PROTEIN; INTEGRITY; PATHWAY; GENE; GLYCOSYLATION; oligosaccharyltransferase; protein glycosylation; endoplasmic reticulum; dolichol; Saccharomyces cerevisiae |
| Subjects: | 500 Science > 580 Botanical sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Apr 2021 12:16 |
| Last Modified: | 12 Apr 2021 12:16 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35322 |
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