Oligosaccharyltransferase is a multiprotein complex that catalyzes asparagine-linked
glycosylation of diverse proteins. Using yeast genetics and glycoproteomics, we found that
transient interactions between nascent polypeptide and Ost3p/Ost6p, homologous subunits
of oligosaccharyltransferase, were able to modulate glycosylation efficiency in a site-specific
manner in vivo. These interactions were driven by hydrophobic and electrostatic
complementarity between amino acids in the peptide-binding groove of Ost3p/Ost6p and the …