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Glycobiology vol 6 no 5 pp. 493-498, 1996
© 1996

research-article

Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway

Gilles Reiss, Stephen te Heesen, Jenet Zimmerman1, Phillips Robbins1 and Markus Aebi2

Mikrobiologisches Institut, Eidgenössische Technische Hochschule ETH Zentrum, CH-8092 Zürich, Switzerland
Center for Cancer Research. Massachusetts Institute of Technology Cambridge, MA 02139, USA

To whom correspondence be addressed

Received on January 16, 1996; revised on February 26, 1996; accepted on March 13, 1996

N-Linked protein glycosylation in most eukaryotic cells initiates with the transfer of the oligosaccharide Glc3Man9GlcNAc2 from the lipid carrier dolichyl pyrophosphate to selected asparagine residues. In the yeast Saccharomyces cerevisiae, alg mutations which affect the assembly of the lipid-linked oligosaccharide at the membrane of the endoplasmic reticulum result in the accumulation of lipid-linked oligosaccharide intermediates and a hypoglycosylation of proteins. Exploiting the synthetic growth defect of alg mutations in combination with mutations affecting oligosaccharyl transferase activity (Stagljar et al., 1994), we have isolated the ALG6 locus. alg6 mutants accumulate lipid-linked Man9GlcNAc2, suggesting that this locus encodes an endoplasmic glucosyltransferase. Alg6p has sequence similarity to Alg8p, a protein required for glucosylation of Glc1Man9GlcNAc2.

Saccharomyces cerevisiae endoplasmic reticulum glycosyltransferase dolichol


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