Skip Navigation


Glycobiology Advance Access originally published online on March 1, 2006
Glycobiology 2006 16(6):91R-101R; doi:10.1093/glycob/cwj099
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
16/6/91R    most recent
cwj099v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Weerapana, E.
Right arrow Articles by Imperiali, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Weerapana, E.
Right arrow Articles by Imperiali, B.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

REVIEW

Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems

Eranthie Weerapana and Barbara Imperiali1

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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
F. P. Nasab, B. L. Schulz, F. Gamarro, A. J. Parodi, and M. Aebi
All in One: Leishmania major STT3 Proteins Substitute for the Whole Oligosaccharyltransferase Complex in Saccharomyces cerevisiae
Mol. Biol. Cell, September 1, 2008; 19(9): 3758 - 3768.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
N. Averbeck, X.-D. Gao, S.-I. Nishimura, and N. Dean
Alg13p, the Catalytic Subunit of the Endoplasmic Reticulum UDP-GlcNAc Glycosyltransferase, Is a Target for Proteasomal Degradation
Mol. Biol. Cell, May 1, 2008; 19(5): 2169 - 2178.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
N. Sharon
Celebrating the golden anniversary of the discovery of bacillosamine, the diamino sugar of a Bacillus,
Glycobiology, November 1, 2007; 17(11): 1150 - 1155.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Averbeck, S. Keppler-Ross, and N. Dean
Membrane Topology of the Alg14 Endoplasmic Reticulum UDP-GlcNAc Transferase Subunit
J. Biol. Chem., October 5, 2007; 282(40): 29081 - 29088.
[Abstract] [Full Text] [PDF]

Home page
 J. Dent. Res.Home page
E.J. Helmerhorst and F.G. Oppenheim
Saliva: a Dynamic Proteome
J. Dent. Res., August 1, 2007; 86(8): 680 - 693.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Sharon
Lectins: Carbohydrate-specific Reagents and Biological Recognition Molecules
J. Biol. Chem., February 2, 2007; 282(5): 2753 - 2764.
[Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.