TY - JOUR
T1 - Add salt, add sugar
T2 - N-glycosylation in Haloferax volcanii
AU - Kaminski, Lina
AU - Naparstek, Shai
AU - Kandiba, Lina
AU - Cohen-Rosenzweig, Chen
AU - Arbiv, Adi
AU - Konrad, Zvia
AU - Eichler, Jerry
PY - 2013/2/1
Y1 - 2013/2/1
N2 - 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.
AB - 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.
KW - Archaea
KW - Haloferax volcanii
KW - N-glycosylation
KW - Post-translational modification
KW - Proteomic diversity
UR - http://www.scopus.com/inward/record.url?scp=84873167653&partnerID=8YFLogxK
U2 - 10.1042/BST20120142
DO - 10.1042/BST20120142
M3 - Article
C2 - 23356324
AN - SCOPUS:84873167653
SN - 0300-5127
VL - 41
SP - 432
EP - 435
JO - Biochemical Society Transactions
JF - Biochemical Society Transactions
IS - 1
ER -