Sweet New Roles for Protein Glycosylation in Prokaryotes.
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.
Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel. Electronic address: jeichler@bgu.ac.il.
Jerry
J
Eichler
Department of Biosciences, University of Oslo, 0316 Oslo, Norway.
Michael
M
Koomey
D001105:Archaea / Q000235:genetics / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001419:Bacteria / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D011499:Protein Processing, Post-Translational
D019843:Archaeal Proteins; D001426:Bacterial Proteins
Archaea; Bacteria; post-translational modifications; protein glycosylation