TY - JOUR
T1 - Archaeal S-layer glycoproteins
T2 - Post-translational modification in the face of extremes
AU - Kandiba, Lina
AU - Eichler, Jerry
N1 - Funding Information: Research in the Eichler laboratory is supported by the Israel Science Foundation (grant 8/11) and the US Army Research Office (W911NF-11-1-520) Publisher Copyright: © 2014 Kandiba and Eichler.
PY - 2014/1/1
Y1 - 2014/1/1
N2 - Corresponding to the sole or basic component of the surface (S)-layer surrounding the archaeal cell in most known cases, S-layer glycoproteins are in direct contact with the harsh environments that characterize niches where Archaea can thrive. Accordingly, early work examining archaeal S-layer glycoproteins focused on identifying those properties that allow members of this group of proteins to maintain their structural integrity in the face of extremes of temperature, pH, and salinity, as well as other physical challenges. However, with expansion of the list of archaeal strains serving as model systems, as well as growth in the number of molecular tools available for the manipulation of these strains, studies on archaeal S-layer glycoproteins are currently more likely to consider the various post-translational modifications these polypeptides undergo. For instance, archaeal S-layer glycoproteins can undergo proteolytic cleavage, both N- and O-glycosylation, lipid-modification and oligomerization. In this mini-review, recent findings related to the post-translational modification of archaeal S-layer glycoproteins are considered.
AB - Corresponding to the sole or basic component of the surface (S)-layer surrounding the archaeal cell in most known cases, S-layer glycoproteins are in direct contact with the harsh environments that characterize niches where Archaea can thrive. Accordingly, early work examining archaeal S-layer glycoproteins focused on identifying those properties that allow members of this group of proteins to maintain their structural integrity in the face of extremes of temperature, pH, and salinity, as well as other physical challenges. However, with expansion of the list of archaeal strains serving as model systems, as well as growth in the number of molecular tools available for the manipulation of these strains, studies on archaeal S-layer glycoproteins are currently more likely to consider the various post-translational modifications these polypeptides undergo. For instance, archaeal S-layer glycoproteins can undergo proteolytic cleavage, both N- and O-glycosylation, lipid-modification and oligomerization. In this mini-review, recent findings related to the post-translational modification of archaeal S-layer glycoproteins are considered.
KW - Archaea
KW - Lipid modification
KW - Post-translational modification
KW - Protein glycosylation
KW - S-layer glycoprotein
UR - http://www.scopus.com/inward/record.url?scp=84987814226&partnerID=8YFLogxK
U2 - https://doi.org/10.3389/fmicb.2014.00661
DO - https://doi.org/10.3389/fmicb.2014.00661
M3 - Short survey
SN - 1664-302X
VL - 5
JO - Frontiers in Microbiology
JF - Frontiers in Microbiology
IS - NOV
M1 - 661
ER -