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

Biochem Soc Trans. 2013 Feb 1;41(1):432-5. doi: 10.1042/BST20120142.

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-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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Archaeal Proteins / metabolism
  • Carbohydrate Metabolism*
  • Glycosylation
  • Haloferax volcanii / metabolism*
  • Mass Spectrometry
  • Protein Processing, Post-Translational
  • Sodium Chloride / metabolism*

Substances

  • Archaeal Proteins
  • Sodium Chloride