Glycobiology Advance Access originally published online on March 1, 2006
Glycobiology 2006 16(6):91R-101R; doi:10.1093/glycob/cwj099
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Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139
1 To whom correspondence should be addressed; e-mail: imper{at}mit.edu
accepted on February 27, 2006
Asparagine-linked protein glycosylation is a prevalent protein modification reaction in eukaryotic systems. This process involves the co-translational transfer of a pre-assembled tetradecasaccharide from a dolichyl-pyrophosphate donor to the asparagine side chain of nascent proteins at the endoplasmic reticulum (ER) membrane. Recently, the first such system of N-linked glycosylation was discovered in the Gram-negative bacterium, Campylobacter jejuni. Glycosylation in this organism involves the transfer of a heptasaccharide from an undecaprenyl-pyrophosphate donor to the asparagine side chain of proteins at the bacterial periplasmic membrane. Here we provide a detailed comparison of the machinery involved in the N-linked glycosylation systems of eukaryotic organisms, exemplified by the yeast Saccharomyces cerevisiae, with that of the bacterial system in C. jejuni. The two systems display significant similarities and the relative simplicity of the bacterial glycosylation process could provide a model system that can be used to decipher the complex eukaryotic glycosylation machinery.
Key words: Campylobacter jejuni / dolichol pathway / oligosaccharyl transferase / pgl gene cluster / protein glycosylation
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