Abstract
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-translationalmodification 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 nonnative proteins, forms the basis for establishing this species as a glyco-engineering platform. In the present review, these and other recent findings are addressed.
Original language | American English |
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Pages (from-to) | 432-435 |
Number of pages | 4 |
Journal | Biochemical Society Transactions |
Volume | 41 |
Issue number | 1 |
DOIs | |
State | Published - 1 Feb 2013 |
Keywords
- Archaea
- Haloferax volcanii
- N-glycosylation
- Post-translational modification
- Proteomic diversity
All Science Journal Classification (ASJC) codes
- Biochemistry