期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 41, 期 -, 页码 432-435出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST20120142
关键词
Archaea; Haloferax volcanii; N-glycosylation; post-translational modification; proteomic diversity
资金
- Israel Science Foundation [8/11]
- US Army Research Office [W911NF-11-1-520]
- Negev-Zin Associates Scholarship
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.
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