TY - JOUR
T1 - Sweet New Roles for Protein Glycosylation in Prokaryotes
AU - Eichler, Jerry
AU - Koomey, Michael
N1 - Funding Information:
J.E. was supported by grants from the Israel Science Foundation (ISF) (grant 109/16), the ISF within the ISF-UGC joint research program framework (grant 2253/15), the ISF-NSFC joint research program (grant 2193/16) and the German-Israeli Foundation for Scientific Research and Development (grant I-1290-416.13/2015). M.K. was supported in part by Research Council of Norway (RCN) project 214442, as well as the Centre for Integrative Microbial Evolution at the Department of Biosciences, University of Oslo.
Funding Information:
J.E. was supported by grants from the Israel Science Foundation (ISF) (grant 109/16 ), the ISF within the ISF-UGC joint research program framework (grant 2253/15 ), the ISF-NSFC joint research program (grant 2193/16 ) and the German-Israeli Foundation for Scientific Research and Development (grant I-1290-416.13/2015 ). M.K. was supported in part by Research Council of Norway (RCN) project 214442, as well as the Centre for Integrative Microbial Evolution at the Department of Biosciences, University of Oslo.
Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017/8/1
Y1 - 2017/8/1
N2 - Long-held to be a post-translational modification unique to Eukarya, it is now clear that both Bacteria and Archaea also perform protein glycosylation, namely the covalent attachment of mono- to polysaccharides to specific protein targets. At the same time, many of the roles assigned to this protein-processing event in eukaryotes, such as guiding protein folding/quality control, intracellular trafficking, dictating cellular recognition events and others, do not apply or are even irrelevant to prokaryotes. As such, protein glycosylation must serve novel functions in Bacteria and Archaea. Recent efforts have begun to elucidate some of these prokaryote-specific roles, which are addressed in this review. Because many of the roles assumed by protein glycosylation in eukaryotes are not applicable to Bacteria or Archaea, this postmodification likely serves distinct roles in prokaryotes. In Bacteria, protein glycosylation systems are found in nonpathogenic species, pointing to roles beyond virulence. In Bacteria and Archaea, protein glycosylation contributes to the integrity and proper architecture of glycoprotein-containing assemblies. Changes in protein glycosylation offers prokaryotes a rapid and reversible manner in which to respond to environmental changes.
AB - Long-held to be a post-translational modification unique to Eukarya, it is now clear that both Bacteria and Archaea also perform protein glycosylation, namely the covalent attachment of mono- to polysaccharides to specific protein targets. At the same time, many of the roles assigned to this protein-processing event in eukaryotes, such as guiding protein folding/quality control, intracellular trafficking, dictating cellular recognition events and others, do not apply or are even irrelevant to prokaryotes. As such, protein glycosylation must serve novel functions in Bacteria and Archaea. Recent efforts have begun to elucidate some of these prokaryote-specific roles, which are addressed in this review. Because many of the roles assumed by protein glycosylation in eukaryotes are not applicable to Bacteria or Archaea, this postmodification likely serves distinct roles in prokaryotes. In Bacteria, protein glycosylation systems are found in nonpathogenic species, pointing to roles beyond virulence. In Bacteria and Archaea, protein glycosylation contributes to the integrity and proper architecture of glycoprotein-containing assemblies. Changes in protein glycosylation offers prokaryotes a rapid and reversible manner in which to respond to environmental changes.
KW - Archaea
KW - Bacteria
KW - post-translational modifications
KW - protein glycosylation
UR - http://www.scopus.com/inward/record.url?scp=85015789422&partnerID=8YFLogxK
U2 - 10.1016/j.tim.2017.03.001
DO - 10.1016/j.tim.2017.03.001
M3 - Review article
AN - SCOPUS:85015789422
SN - 0966-842X
VL - 25
SP - 662
EP - 672
JO - Trends in Microbiology
JF - Trends in Microbiology
IS - 8
ER -