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Archaea
Volume 2010 (2010), Article ID 612948, 13 pages
http://dx.doi.org/10.1155/2010/612948
Review Article

S-Layer Glycoproteins and Flagellins: Reporters of Archaeal Posttranslational Modifications

1Department of Microbiology and Immunology, Queen's University, Kingston, ON, Canada K7L 3N6
2Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel

Received 8 April 2010; Accepted 15 June 2010

Academic Editor: Joerg Soppa

Copyright © 2010 Ken F. Jarrell et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Many archaeal proteins undergo posttranslational modifications. S-layer proteins and flagellins have been used successfully to study a variety of these modifications, including N-linked glycosylation, signal peptide removal and lipid modification. Use of these well-characterized reporter proteins in the genetically tractable model organisms, Haloferax volcanii, Methanococcus voltae and Methanococcus maripaludis, has allowed dissection of the pathways and characterization of many of the enzymes responsible for these modifications. Such studies have identified archaeal-specific variations in signal peptidase activity not found in the other domains of life, as well as the enzymes responsible for assembly and biosynthesis of novel N-linked glycans. In vitro assays for some of these enzymes have already been developed. N-linked glycosylation is not essential for either Hfx. volcanii or the Methanococcus species, an observation that allowed researchers to analyze the role played by glycosylation in the function of both S-layers and flagellins, by generating mutants possessing these reporters with only partial attached glycans or lacking glycan altogether. In future studies, it will be possible to consider questions related to the heterogeneity associated with given modifications, such as differential or modulated glycosylation.