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9.B.231.  The Die2/ALG10 Glycosyl Transferase (Die2/ALG10) Family 

The biosynthesis of the lipid-linked oligosaccharide substrate for N-linked protein glycosylation follows a highly conserved pathway at the membrane of the endoplasmic reticulum in eukaryotes. Based on the synthetic growth defect in combination with a reduced oligosaccharyltransferase activity (wbp1), Burda and Aebi 1998 identified alg10 mutant strains which accumulate lipid-linked Glc2Man9GlcNAc2. They cloned the corresponding wild-type gene and showed that Alg10p is a dolichyl-phosphoglucose-dependent glucosyltransferase which adds the terminal alpha-1,2 glucose to the lipid-linked Glc2Man9GlcNAc2 oligosaccharide. Hypoglycosylation of secreted proteins in alg10 deletion strains demonstrated that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase. This ensures that completely assembled oligosaccharide is transferred to protein (Burda and Aebi 1998).

References associated with 9.B.231 family:

Burda, P. and M. Aebi. (1998). The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology 8: 455-462. 9597543
Farid, A., M. Pabst, J. Schoberer, F. Altmann, J. Glössl, and R. Strasser. (2011). Arabidopsis thaliana alpha1,2-glucosyltransferase (ALG10) is required for efficient N-glycosylation and leaf growth. Plant J. 68: 314-325. 21707802