ArticleJournal of bacteriology2009
AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 46 citations in OpenAlex.
- Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility.Nature communications · 2024Article
- Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes.eLife · 2022Article
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Identifying Components of aFrontiers in microbiology · 2021Article
- Article
- Identification of a novelThe Journal of biological chemistry · 2020Article
- Article
- Identification and characterization of the 4-epimerase AglW from the archaeon Methanococcus maripaludis.Glycoconjugate journal · 2018Article
- Genomic variation and biogeography of Antarctic haloarchaea.Microbiome · 2018Article
- AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7.Extremophiles : life under extreme conditions · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- The archaellum: how Archaea swim.Frontiers in microbiology · 2015Article
- N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014Review
- Identification of genes involved in the biosynthesis of the third and fourth sugars of the Methanococcus maripaludis archaellin N-linked tetrasaccharide.Journal of bacteriology · 2013Article
- Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.Nature chemical biology · 2013Article
- Agl16, a thermophilic glycosyltransferase mediating the last step of N-Glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.Journal of bacteriology · 2013Article
- Extreme sweetness: protein glycosylation in archaea.Nature reviews. Microbiology · 2013Review
- Surface appendages of archaea: structure, function, genetics and assembly.Life (Basel, Switzerland) · 2013Review
- Bacterial cell-envelope glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2013Review
- Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent advances in the field of prokaryotic N-glycosylation have established a foundation for the pathways and proteins involved in this important posttranslational protein modification process. To continue the study of the Methanococcus voltae N-glycosylation pathway, characteristics of known eukaryotic, bacterial, and archaeal proteins involved in the N-glycosylation process were examined and used to select candidate M. voltae genes for investigation as potential glycosyl transferase and flippase components. The targeted genes were knocked out via linear gene replacement, and the resulting effects on N-glycan assembly were identified through flagellin and surface (S) layer protein glycosylation defects. This study reports the finding that deletion of two putative M. voltae glycosyl transferase genes, designated aglC (for archaeal glycosylation) and aglK, interfered with proper N-glycosylation. This resulted in flagellin and S-layer proteins with significantly reduced apparent molecular masses, loss of flagellar assembly, and absence of glycan attachment. Given previous knowledge of both the N-glycosylation pathway in M. voltae and the general characteristics of N-glycosylation components, it appears that AglC and AglK are involved in the biosynthesis or transfer of diacetylated glucuronic acid within the glycan structure. In addition, a knockout of the putative flippase candidate gene (Mv891) had no effect on N-glycosylation but did result in the production of giant cells with diameters three to four times that of wild-type cells.
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Registered trials
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