Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway |
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Authors: | Reiss Gilles; Heesen Stephen te; Zimmerman Jenet; Robbins Phillips; Aebi Markus |
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Institution: | Mikrobiologisches Institut, Eidgenössische Technische Hochschule ETH Zentrum, CH-8092 Zürich, Switzerland
Center for Cancer Research. Massachusetts Institute of Technology Cambridge, MA 02139, USA |
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Abstract: | N-Linked protein glycosylation in most eukaryotic cells initiateswith the transfer of the oligosaccharide Glc3Man9GlcNAc2 fromthe lipid carrier dolichyl pyrophosphate to selected asparagineresidues. In the yeast Saccharomyces cerevisiae, alg mutationswhich affect the assembly of the lipid-linked oligosaccharideat the membrane of the endoplasmic reticulum result in the accumulationof lipid-linked oligosaccharide intermediates and a hypoglycosylationof proteins. Exploiting the synthetic growth defect of alg mutationsin combination with mutations affecting oligosaccharyl transferaseactivity (Stagljar et al., 1994), we have isolated the ALG6locus. alg6 mutants accumulate lipid-linked Man9GlcNAc2, suggestingthat this locus encodes an endoplasmic glucosyltransferase.Alg6p has sequence similarity to Alg8p, a protein required forglucosylation of Glc1Man9GlcNAc2. Saccharomyces cerevisiae endoplasmic reticulum glycosyltransferase dolichol |
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