Add salt, add sugar: N-glycosylation in Haloferax volcanii

• Published in: Biochemical Society transactions Vol. 41; no. 1; p. 432
• Main Authors: Kaminski, Lina, Naparstek, Shai, Kandiba, Lina, Cohen-Rosenzweig, Chen, Arbiv, Adi, Konrad, Zvia, Eichler, Jerry
• Format: Journal Article
• Language: English
• Published: England 01-02-2013
• Subjects: Archaeal Proteins - metabolism; Carbohydrate Metabolism; Glycosylation; Haloferax volcanii - metabolism; Mass Spectrometry; Protein Processing, Post-Translational; Sodium Chloride - metabolism
• ISSN: 1470-8752
• DOI: 10.1042/BST20120142

Although performed by members of all three domains of life, the archaeal version of N-glycosylation remains the least understood. Studies on Haloferax volcanii have, however, begun to correct this situation. A combination of bioinformatics, molecular biology, biochemical and mass spectrometry approaches have served to delineate the Agl pathway responsible for N-glycosylation of the S-layer glycoprotein, a reporter of this post-translational modification in Hfx. volcanii. More recently, differential N-glycosylation of the S-layer glycoprotein as a function of environmental salinity was demonstrated, showing that this post-translational modification serves an adaptive role in Hfx. volcanii. Furthermore, manipulation of the Agl pathway, together with the capability of Hfx. volcanii to N-glycosylate non-native proteins, forms the basis for establishing this species as a glyco-engineering platform. In the present review, these and other recent findings are addressed.