Add salt, add sugar: N-glycosylation in Haloferax volcanii.
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.
Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
Lina
L
Kaminski
Shai
S
Naparstek
Lina
L
Kandiba
Chen
C
Cohen-Rosenzweig
Adi
A
Arbiv
Zvia
Z
Konrad
Jerry
J
Eichler
D019843:Archaeal Proteins / Q000378:metabolism; D050260:Carbohydrate Metabolism; D006031:Glycosylation; D019622:Haloferax volcanii / Q000378:metabolism*; D013058:Mass Spectrometry; D011499:Protein Processing, Post-Translational; D012965:Sodium Chloride / Q000378:metabolism*
D019843:Archaeal Proteins; D012965:Sodium Chloride