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Glycobiology Advance Access originally published online on January 7, 2009
Glycobiology 2009 19(5):472-478; doi:10.1093/glycob/cwp001
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle

Christine Noffz2, Sabine Keppler-Ross2 and Neta Dean2,1

2 Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA

1 To whom correspondence should be addressed: Tel: +1-631-632-9309; Fax: +1-631-632-8575; e-mail: neta.dean{at}stonybrook.edu

Received on October 16, 2008; revised on January 2, 2009; accepted on January 3, 2009

N-Linked glycosylation begins with the formation of a dolichol-linked oligosaccharide in the endoplasmic reticulum (ER). The first two steps of this pathway lead to the formation of GlcNAc2-PP-dolichol, whose synthesis is sequentially catalyzed by the Alg7p GlcNAc phosphotransferase and by the dimeric Alg13p/Alg14p UDP-GlcNAc transferase on the cytosolic face of the endoplasmic reticulum. Here, we show that the Alg7p, Alg13p, and Alg14p glycosyltransferases form a functional multienzyme complex. Coimmunoprecipitation and gel filtration assays demonstrate that the Alg7p/Alg13p/Alg14p complex is a hexamer with a native molecular weight of ~200 kDa and an Alg7p:Alg13:Alg14p stoichiometry of 1:1:1. These results highlight and extend the striking parallels that exist between these eukaryotic UDP-GlcNAc transferases and their bacterial MraY and MurG homologs that catalyze the first two steps of the lipid-linked peptidoglycan precursor. In addition to their preferred substrate and lipid acceptors, these enzymes are similar in their structure, chemistry, temporal, and spatial organization. These similarities point to an evolutionary link between the early steps of N-linked glycosylation and those of peptidoglycan synthesis.

Key words: endoplasmic reticulum / glycosylation / lipid-linked oligosaccharide / peptidoglycan / UDP-GlcNAc glycosyltransferase


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