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...

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Veröffentlicht in:Trends in microbiology (Regular ed.) 2017-08, Vol.25 (8), p.662-672
Hauptverfasser: Eichler, Jerry, Koomey, Michael
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0966-842X
1878-4380
DOI:10.1016/j.tim.2017.03.001