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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 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 homologs indicates that they are ancient in Eukaryotes, either as a lateral transfer or inherited through eukaryogenesis.
Original language | English |
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Article number | e67448 |
Number of pages | 27 |
Journal | eLife |
Volume | 11 |
DOIs | |
Publication status | Published - 8 Apr 2022 |
Keywords
- Agl24
- Alg13
- Alg14
- E. coli
- N-glycosylation
- Sulfolobus acidocladarius
- biochemistry
- chemical biology
- chitobiose
- infectious disease
- microbiology
ASJC Scopus subject areas
- General Neuroscience
- General Biochemistry,Genetics and Molecular Biology
- General Immunology and Microbiology
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Dive into the research topics of 'Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes'. Together they form a unique fingerprint.Projects
- 1 Finished
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Functional and Structural Studies of the Streptococcal Virulence Factor Group A Carbohydrate Biosynthesis Pathway (Sir Henry Dale Fellowship)
Dorfmueller, H. (Investigator)
1/04/16 → 30/06/22
Project: Research