Cited by 12Glycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisFungal and yeast genetics research

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Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes

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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 a rchaeal gl ycosylation 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 homologs indicates that they are ancient in Eukaryotes, either as a lateral transfer or inherited through eukaryogenesis.

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Metadata

Authors
Meyer, B. H., Adam, P. S., Wagstaff, B. A., Kolyfetis, G. E., Probst, A. J., Albers, S. V., & Dorfmueller, H. C.
Affiliations
  • University of Freiburg (DE)
  • University of Duisburg-Essen (DE)
  • University of Dundee (GB)
  • National and Kapodistrian University of Athens (GR)
Corresponding author
  • Meyer, Benjamin H
  • Dorfmueller, Helge C
Venue
eLife
Published
2022-04-08
Volume
11
ISSN
2050-084X (ISSN-L)
OpenAlex
W4223452448
Cited by
12
References
5
Citations by year
2026: 2 · 2025: 4 · 2024: 4 · 2023: 1 · 2022: 1
FWCI
0.82
Type
journal article
Language
en
Open access
Locations
  • eLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Discovery Research Portal (University of Dundee) (submittedVersion, cc-by)
  • Universitätsbibliographie, Universität Duisburg-Essen (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • KOPS (University of Konstanz) (submittedVersion, cc-by)
Funders
  • The Wellcome Trust and Royal Society Grant (109357/Z/15/Z)
  • SFG (403222702-SFB 1381)
  • Ministerium für Kultur und Wissenschaft des Landes Nordrhein-Westfalen (Nachwuchsgruppe Dr. Alexander Probst)
  • Alexander von Humboldt Foundation (Postdoctoral fellowship)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords
AGL24, lipid-linked oligosaccharides, crenarchaeon, MurG, eukaryotic origin, horizontal gene transfer, protein evolution, phylogenetic analysis, structural modeling
MeSH terms
Archaea, Disaccharides, Phylogeny, Polysaccharides, Eukaryota

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