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http://purl.uniprot.org/citations/25118247http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25118247http://www.w3.org/2000/01/rdf-schema#comment"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 sequestered stretch of substrate polypeptide. Based on this dependence, we used in vivo scanning mutagenesis and in vitro biochemistry to map the precise interactions that affect site-specific glycosylation efficiency. We conclude that transient binding of substrate polypeptide by Ost3p/Ost6p increases glycosylation efficiency at asparagines proximal and C-terminal to sequestered sequences. We detail a novel mode of interaction between translocating nascent polypeptide and oligosaccharyltransferase in which binding to Ost3p/Ost6p segregates a short flexible loop of glycosylation-competent polypeptide substrate that is delivered to the oligosaccharyltransferase active site for efficient modification."xsd:string
http://purl.uniprot.org/citations/25118247http://purl.org/dc/terms/identifier"doi:10.1074/mcp.m114.041178"xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/author"Schulz B.L."xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/author"Bailey U.M."xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/author"Jamaluddin M.F."xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/name"Mol Cell Proteomics"xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/pages"3286-3293"xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/title"Oligosaccharyltransferase subunits bind polypeptide substrate to locally enhance N-glycosylation."xsd:string
http://purl.uniprot.org/citations/25118247http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/25118247http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25118247
http://purl.uniprot.org/citations/25118247http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25118247
http://purl.uniprot.org/uniprot/#_A0A6A5PSN4-mappedCitation-25118247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/#_A0A6A5Q3S9-mappedCitation-25118247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/#_Q03723-mappedCitation-25118247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/#_P48439-mappedCitation-25118247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/A0A6A5Q3S9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/P48439http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/A0A6A5PSN4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25118247
http://purl.uniprot.org/uniprot/Q03723http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25118247