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Glycobiology Advance Access first published online on January 7, 2009
This version published online on January 7, 2009
Glycobiology, 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 Noffz, Sabine Keppler-Ross and Neta Dean*

Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794–5215

* Address correspondence to: Neta Dean, email: Neta.Dean{at}stonybrook.edu, (TEL) 631–632-9309, (FAX) 631–632-8575

Received on October 16, 2008; 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 leads 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 multi-enzyme complex. Co-immunoprecipitation and gel filtration assays demonstrate that the Alg7p/Alg13p/Alg14p complex is a hexamer with a native molecular weight of ~200 kDa and a 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 homologues 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: glycosylation / endoplasmic reticulum / UDP-GlcNAc glycosyltransferase / lipid-linked oligosaccharide / peptidoglycan

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