OST Complex (OST48, Ribophorin I, Ribophorin II, DAD1)

  • Yoichiro Harada
  • Tadashi Suzuki
Reference work entry


Protein N-glycosylation is now found in all three domains of life (Kelleher and Gilmore 2006; Schwarz and Aebi 2011). The common features of this protein modification throughout the evolution are the preassembly of the N-glycan precursors on the lipid carriers (dolichol, Dol for eukaryote and archaea, undecaprenol for bacteria) and its transfer to nascent polypeptides. In Saccharomyces cerevisiae and mammals, the preassembly of the glycan begins with the synthesis of the Man5GlcNAc2-PP-Dol (PP stands for pyrophosphate) intermediate on the cytosolic side of the endoplasmic reticulum (ER) membrane, which is then flipped into the ER lumen to be matured to the fully assembled Glc3Man9GlcNAc2-PP-Dol. The oligosaccharide moiety is transferred en bloc to the side chain of asparagine residue within the N-glycosylation consensus sequences (N-X-S/T, X ≠ P) of nascent polypeptides in the ER lumen. The N-glycosylation reaction is catalyzed by oligosaccharyltransferase (OST), the multi-membrane protein complex associated with the ER membrane. The catalytic center of OST resides in the Stt3 proteins that are conserved throughout evolution. In mammals and S. cerevisiae, the Stt3 proteins need to form a complex for the maximum activity with the accessory membrane proteins (DDOST/OST48, RPN1/ribophorin I, RPN2/ribophorin II, DAD1, Ost4, TUSC3/N33, and MGAT1/IAP in mammals; Wbp1, Swp1, Ost1, Ost2, Ost4, Ost5, and either Ost3 or its paralog Ost6 in S. cerevisiae). On the other hand, some pathogenic bacteria and protists contain only Stt3 orthologs.


Endoplasmic Reticulum Membrane Endoplasmic Reticulum Lumen Nascent Polypeptide Glycosyl Donor Endoplasmic Reticulum Retention Signal 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.Glycometabolome Team, Systems Glycobiology Research GroupRIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKENWakoJapan

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