Sweet New Roles for Protein Glycosylation in Prokaryotes

Trends Microbiol. 2017 Aug;25(8):662-672. doi: 10.1016/j.tim.2017.03.001. Epub 2017 Mar 21.

Abstract

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.

Keywords: Archaea; Bacteria; post-translational modifications; protein glycosylation.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea / genetics
  • Archaea / metabolism*
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism*
  • Bacteria / genetics
  • Bacteria / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Glycosylation
  • Protein Processing, Post-Translational*

Substances

  • Archaeal Proteins
  • Bacterial Proteins