TY - JOUR
T1 - N-glycosylation in Haloferax volcanii
T2 - Adjusting the sweetness
AU - Eichler, Jerry
AU - Arbiv, Adi
AU - Cohen-Rosenzweig, Chen
AU - Kaminski, Lina
AU - Kandiba, Lina
AU - Konrad, Zvia
PY - 2013/1/1
Y1 - 2013/1/1
N2 - Long believed to be restricted to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans to select target protein asparagine residues. Still, it is only in the last decade that pathways of N-glycosylation in Archaea have been delineated. In the haloarchaeon Haloferax volcanii, a series of Agl (archaeal glycosylation) proteins is responsible for the addition of an N-linked pentasaccharide to modified proteins, including the surface (S)-layer glycoprotein, the sole component of the surface layer surrounding the cell. The S-layer glycoprotein N-linked glycosylation profile changes, however, as a function of surrounding salinity. Upon growth at different salt concentrations, the S-layer glycoprotein is either decorated by the N-linked pentasaccharide introduced above or by both this pentasaccharide as well as a tetrasaccharide of distinct composition. Recent efforts have identified Agl5-Agl15 as components of a second Hfx. volcanii N-glycosylation pathway responsible for generating the tetrasaccharide attached to S-layer glycoprotein when growth occurs in 1.75 M but not 3.4 M NaCl-containing medium.
AB - Long believed to be restricted to Eukarya, it is now known that cells of all three domains of life perform N-glycosylation, the covalent attachment of glycans to select target protein asparagine residues. Still, it is only in the last decade that pathways of N-glycosylation in Archaea have been delineated. In the haloarchaeon Haloferax volcanii, a series of Agl (archaeal glycosylation) proteins is responsible for the addition of an N-linked pentasaccharide to modified proteins, including the surface (S)-layer glycoprotein, the sole component of the surface layer surrounding the cell. The S-layer glycoprotein N-linked glycosylation profile changes, however, as a function of surrounding salinity. Upon growth at different salt concentrations, the S-layer glycoprotein is either decorated by the N-linked pentasaccharide introduced above or by both this pentasaccharide as well as a tetrasaccharide of distinct composition. Recent efforts have identified Agl5-Agl15 as components of a second Hfx. volcanii N-glycosylation pathway responsible for generating the tetrasaccharide attached to S-layer glycoprotein when growth occurs in 1.75 M but not 3.4 M NaCl-containing medium.
KW - Archaea
KW - Haloferax volcanii
KW - N-glycosylation
KW - Post-translational modification
KW - Protein glycosylation
KW - S-layer glycoprotein
UR - http://www.scopus.com/inward/record.url?scp=84892175040&partnerID=8YFLogxK
U2 - 10.3389/fmicb.2013.00403
DO - 10.3389/fmicb.2013.00403
M3 - Short survey
C2 - 24399998
AN - SCOPUS:84892175040
SN - 1664-302X
VL - 4
JO - Frontiers in Microbiology
JF - Frontiers in Microbiology
IS - DEC
ER -