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| FEBS Lett. Dec (2005); 579(29):6564-8 | |
| Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit- | |
| Schwarz M, Knauer R, Lehle L | |
| Lehrstuhl fur Zellbiologie und Pflanzenphysiologie, Universitat Regensburg, Universitatsstrasse 31, 93053 Regensburg, Germany- | |
| Abstract: 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-Thr-sequences 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- | |
| [PUBMED: 16297388] |   |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |