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Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site.

Oligosaccharyltransferase (OT) transfers high mannose-type glycans to the nascent polypeptides that are translated by the membrane-bound ribosome and translocated into the lumen of the endoplasmic reticulum through the Sec61 translocon complex. In this article, we show that purified ribosomes and OT can form a binary complex with a stoichiometry of approximately 1 to 1 in the presence of detergent. We present evidence that OT may bind to the large ribosomal subunit near the site where nascent polypeptides exit. We further show that OT and the Sec61 complex can simultaneously bind to ribosomes in vitro. Based on existing data and our findings, we propose that cotranslational translocation and N-glycosylation of nascent polypeptides are mediated by a ternary supramolecular complex consisting of OT, the Sec61 complex, and ribosomes.

Pubmed ID: 19365066


  • Harada Y
  • Li H
  • Li H
  • Lennarz WJ


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

April 28, 2009

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM33185
  • Agency: NIGMS NIH HHS, Id: GM74985
  • Agency: NIGMS NIH HHS, Id: R01 GM074985

Mesh Terms

  • Binding Sites
  • Biocatalysis
  • Biological Transport
  • Hexosyltransferases
  • Membrane Proteins
  • Membrane Transport Proteins
  • Microscopy, Electron
  • Protein Binding
  • Ribosomes
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins