N-glycosylation in Archaea-New roles for an ancient posttranslational modification

Mol Microbiol. 2020 Nov;114(5):735-741. doi: 10.1111/mmi.14569. Epub 2020 Jul 26.

Abstract

Genome analysis points to N-glycosylation as being an almost universal posttranslational modification in Archaea. Although such predictions have been confirmed in only a limited number of species, such studies are making it increasingly clear that the N-linked glycans which decorate archaeal glycoproteins present diversity in terms of both glycan composition and architecture far beyond what is seen in the other two domains of life. In addition to continuing to decipher pathways of N-glycosylation, recent efforts have revealed how Archaea exploit this variability in novel roles. As well as encouraging glycoprotein synthesis, folding and assembly into properly functioning higher ordered complexes, N-glycosylation also provides Archaea with a strategy to cope with changing environments. Archaea can, moreover, exploit the apparent species-specific nature of N-glycosylation for selectivity in mating, and hence, to maintain species boundaries, and in other events where cell-selective interactions are required. At the same time, addressing components of N-glycosylation pathways across archaeal phylogeny offers support for the concept of an archaeal origin for eukaryotes. In this MicroReview, these and other recent discoveries related to N-glycosylation in Archaea are considered.

Keywords: Archaea; N-glycosylation; evolution; extremophile; posttranslational modification.

Publication types

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

MeSH terms

  • Archaea / metabolism*
  • Archaeal Proteins / metabolism
  • Biological Evolution
  • Evolution, Molecular
  • Genes, Archaeal / genetics
  • Glycoproteins / metabolism
  • Glycosylation*
  • Polysaccharides / genetics
  • Polysaccharides / metabolism*
  • Protein Processing, Post-Translational / genetics
  • Protein Processing, Post-Translational / physiology

Substances

  • Archaeal Proteins
  • Glycoproteins
  • Polysaccharides