@article{3219676,
    title = "Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes",
    author = "Meyer, B.H. and Adam, P.S. and Wagstaff, B.A. and Kolyfetis, G.E. and Probst, A.J. and Albers, S.V. and Dorfmueller, H.C.",
    journal = "eLife",
    year = "2022",
    volume = "11",
    publisher = "eLife Sciences Publications Ltd",
    doi = "10.7554/eLife.67448",
    keywords = "arabinose;  bacterial enzyme;  calcium chloride;  chitobiose;  dextrin;  DNA fragment;  dolichol phosphate;  gellan;  glycan;  histidine;  magnesium chloride;  n acetylglucosamine;  n acetylglucosaminyltransferase;  sulfuric acid;  uracil;  uridine diphosphate, amino acid sequence;  antibiotic resistance;  archaeon;  Article;  bacterium isolate;  bioinformatics;  chromatography;  controlled study;  cryoelectron microscopy;  crystal structure;  crystallography;  electron impact mass spectrometry;  enzyme activity;  gene disruption;  gene fusion;  gene sequence;  glycosylation;  heteronuclear single quantum coherence;  hidden Markov model;  high performance liquid chromatography;  immunoblotting;  kinetic parameters;  mass fragmentography;  nonhuman;  phylogeny;  plasmid;  polymerase chain reaction;  protein expression;  sequence alignment;  sequence homology;  spectroscopy;  substitution reaction",
    abstract = "Protein N-glycosylation is a post-translational modification found in organisms of all domains of life. The crenarchaeal N-glycosylation begins with the synthesis of a lipid-linked chitobiose core structure, identical to that in Eukaryotes, although the enzyme catalyzing this reaction remains unknown. Here, we report the identification of a thermostable archaeal β-1,4-N-acetylglucosaminyltransferase, named archaeal glycosylation enzyme 24 (Agl24), responsible for the synthesis of the N-glycan chitobiose core. Biochemical characterization confirmed its function as an inverting β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol glycosyltransferase. Substitution of a conserved histidine residue, found also in the eukaryotic and bacterial homologs, demonstrated its functional importance for Agl24. Furthermore, bioinformatics and structural modeling revealed similarities of Agl24 to the eukaryotic Alg14/13 and a distant relation to the bacterial MurG, which are catalyzing the same or a similar reaction, respectively. Phylogenetic analysis of Alg14/13 homo-logs indicates that they are ancient in Eukaryotes, either as a lateral transfer or inherited through eukaryogenesis. ‍© Meyer et al."
}