دورية أكاديمية
Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes.
العنوان: | Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes. |
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المؤلفون: | Meyer BH; Environmental Microbiology and Biotechnology (EMB), Aquatic Microbial Ecology, University of Duisburg-Essen, Essen, Germany.; Division of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, United Kingdom.; Molecular Biology of Archaea, Faculty of Biology, University of Freiburg, Freiburg, Germany., Adam PS; Group for Aquatic Microbial Ecology, Environmental Microbiology and Biotechnology, Faculty of Chemistry University Duisburg-Essen, Essen, Germany., Wagstaff BA; Division of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, United Kingdom., Kolyfetis GE; Department of Biochemistry and Molecular Biology, Faculty of Biology, National and Kapodistrian University of Athens, Athens, Greece., Probst AJ; Centre of Water and Environmental Research (ZWU), University of Duisburg-Essen, Essen, Germany., Albers SV; Molecular Biology of Archaea, Faculty of Biology, University of Freiburg, Freiburg, Germany., Dorfmueller HC; Division of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, United Kingdom. |
المصدر: | ELife [Elife] 2022 Apr 08; Vol. 11. Date of Electronic Publication: 2022 Apr 08. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012- |
مواضيع طبية MeSH: | Archaea*/genetics , Eukaryota*, Disaccharides ; Phylogeny ; Polysaccharides |
مستخلص: | 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. Competing Interests: BM, PA, BW, GK, AP, SA, HD No competing interests declared (© 2022, Meyer et al.) |
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معلومات مُعتمدة: | 109357/Z/15/Z The Wellcome Trust and Royal Society Grant; United Kingdom WT_ Wellcome Trust; 105606/Z/14/Z United Kingdom WT_ Wellcome Trust |
فهرسة مساهمة: | Keywords: Agl24; Alg13; Alg14; E. coli; N-glycosylation; Sulfolobus acidocladarius; biochemistry; chemical biology; chitobiose; infectious disease; microbiology |
المشرفين على المادة: | 0 (Disaccharides) 0 (Polysaccharides) 577-76-4 (chitobiose) |
تواريخ الأحداث: | Date Created: 20220408 Date Completed: 20220412 Latest Revision: 20240826 |
رمز التحديث: | 20240826 |
مُعرف محوري في PubMed: | PMC8993221 |
DOI: | 10.7554/eLife.67448 |
PMID: | 35394422 |
قاعدة البيانات: | MEDLINE |
تدمد: | 2050-084X |
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DOI: | 10.7554/eLife.67448 |