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

Link to Article in PubMed

PubMed ID

1555242

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