R. Pathak et al., THE ESSENTIAL YEAST NLT1 GENE ENCODES THE 64-KDA GLYCOPROTEIN SUBUNITOF THE OLIGOSACCHARYL TRANSFERASE, FEBS letters, 362(2), 1995, pp. 229-234
The yeast oligosaccharyl transferase catalyzes the glycosylation of as
paragine residues in secreted, vesicular, and membrane proteins, A com
plex of at least four membrane-bound polypeptides is responsible for o
ligosaccharyl transferase activity, Amino acid sequences from the 64 k
Da glycoprotein subunit of the complex were used to clone the essentia
l NLT1 (N-linked oligosaccharyl transferase) gene, The Nlt1p gene prod
uct is a processed, multiply glycosylated type I membrane protein; it
has an extensive amino-terminal soluble domain, a potential hydrophobi
c transmembrane domain, and a short carboxy-terminal soluble domain, T
he Nlt1p is significantly similar than the mammalian ribophorin I, a c
omponent of the mammalian oligosaccharyl transferase complex, and the
enzyme is conserved throughout eukaryotic evolution.