title: Phylogenetic- and genome-derived insight into the evolution of N-glycosylation in Archaea.
abstract: N-glycosylation, the covalent attachment of oligosaccharides to target protein Asn residues, is a post-translational modification that occurs in all three domains of life. In Archaea, the N-linked glycans that decorate experimentally characterized glycoproteins reveal a diversity in composition and content unequaled by their bacterial or eukaryal counterparts. At the same time, relatively little is known of archaeal N-glycosylation pathways outside of a handful of model strains. To gain insight into the distribution and evolutionary history of the archaeal version of this universal protein-processing event, 168 archaeal genome sequences were scanned for the presence of aglB, encoding the known archaeal oligosaccharyltransferase, an enzyme key to N-glycosylation. Such analysis predicts the presence of AglB in 166 species, with some species seemingly containing multiple versions of the protein. Phylogenetic analysis reveals that the events leading to aglB duplication occurred at various points during archaeal evolution. In many cases, aglB is found as part of a cluster of putative N-glycosylation genes. The presence, arrangement and nucleotide composition of genes in aglB-based clusters in five species of the halophilic archaeon Haloferax points to lateral gene transfer as contributing to the evolution of archaeal N-glycosylation.
authors.affiliation: Department of Life Sciences, Ben Gurion University, Beersheva 84105, Israel.
authors.forename: Lina
authors.initials: L
authors.lastname: Kaminski
authors.forename: Mor N
authors.initials: MN
authors.lastname: Lurie-Weinberger
authors.forename: Thorsten
authors.initials: T
authors.lastname: Allers
authors.forename: Uri
authors.initials: U
authors.lastname: Gophna
authors.forename: Jerry
authors.initials: J
authors.lastname: Eichler
mesh_terms: D001105:Archaea / Q000201:enzymology / Q000235:genetics; D019843:Archaeal Proteins / Q000235:genetics* / Q000378:metabolism; D003062:Codon; D019143:Evolution, Molecular; D020440:Gene Duplication; D022761:Gene Transfer, Horizontal; D020745:Genome, Archaeal; D006023:Glycoproteins / Q000235:genetics* / Q000378:metabolism; D006031:Glycosylation; D019621:Haloferax / Q000201:enzymology / Q000235:genetics*; D006602:Hexosyltransferases / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics; D005810:Multigene Family; D010802:Phylogeny; D011499:Protein Processing, Post-Translational / Q000235:genetics*
chemical_list: D019843:Archaeal Proteins; D003062:Codon; D006023:Glycoproteins; D008565:Membrane Proteins; D006602:Hexosyltransferases; C025620:dolichyl-diphosphooligosaccharide - protein glycotransferase