Title
Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein
UMMS Affiliation
Department of Biochemistry and Molecular Biology
Publication Date
1992-04-03
Document Type
Article
Subjects
Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Chromatography; Consensus Sequence; Dogs; Dolichol; Endoplasmic Reticulum; *Hexosyltransferases; Macromolecular Substances; Membrane Proteins; Molecular Sequence Data; Protein Conformation; Transferases
Disciplines
Biochemistry | Biochemistry, Biophysics, and Structural Biology | Cell Biology | Molecular Biology
Abstract
Oligosaccharyltransferase catalyzes the N-linked glycosylation of asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum (RER). A protein complex composed of 66, 63, and 48 kd subunits copurified with oligosaccharyltransferase from canine pancreas. The 66 and 63 kd subunits were shown by protein immunoblotting to be identical to ribophorin I and II, two previously identified RER glycoproteins that colocalize with membrane-bound ribosomes. The transmembrane segment of ribophorin I was found to be homologous to a recently proposed dolichol recognition consensus sequence. Based on a revision of the consensus sequence, we propose a model for the interaction of dolichol with the glycosyltransferases that catalyze the assembly and transfer of lipid-linked oligosaccharides.
Source
Cell. 1992 Apr 3;69(1):55-65.
Journal/Book/Conference Title
Cell
Related Resources
PubMed ID
1555242
Repository Citation
Kelleher, Daniel J.; Kreibich, Gert; and Gilmore, Reid, "Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein" (1992). Biochemistry and Molecular Pharmacology Publications and Presentations. 189.
https://escholarship.umassmed.edu/bmp_pp/189