ArticleBiochimica et biophysica acta2012
AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.
Article in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Proteome characterization of single gene deletion mutants lacking zinc finger µ-proteins inmicroLife · 2026Article
- Article
- Agl28 and Agl29 are key components of a Halobacterium salinarum N-glycosylation pathway.FEMS microbiology letters · 2023Article
- Distinct Regions of the Haloferax volcanii Dolichol Phosphate-Mannose Synthase AglD Mediate the Assembly and Subsequent Processing of the Lipid-Linked Mannose.Journal of bacteriology · 2022Article
- Insights into gene expression changes under conditions that facilitate horizontal gene transfer (mating) of a model archaeon.Scientific reports · 2020Article
- Biogenesis of Asparagine-Linked Glycoproteins Across Domains of Life-Similarities and Differences.ACS chemical biology · 2018Article
- Article
- Lipid sugar carriers at the extremes: The phosphodolichols Archaea use in N-glycosylation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- N-Glycosylation Is Important for Proper Haloferax volcanii S-Layer Stability and Function.Applied and environmental microbiology · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Archaeal S-Layers: Overview and Current State of the Art.Frontiers in microbiology · 2017Review
- Evidence that biosynthesis of the second and third sugars of the archaellin Tetrasaccharide in the archaeon Methanococcus maripaludis occurs by the same pathway used by Pseudomonas aeruginosa to make a di-N-acetylated sugar.Journal of bacteriology · 2015Article
- Deciphering a pathway of Halobacterium salinarum N-glycosylation.MicrobiologyOpen · 2015Article
- N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014Review
- N-glycosylation in Haloferax volcanii: adjusting the sweetness.Frontiers in microbiology · 2013Article
- Article
- 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
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- Extreme sweetness: protein glycosylation in archaea.Nature reviews. Microbiology · 2013Review
- Bacterial cell-envelope glycoconjugates.Advances in carbohydrate chemistry and biochemistry · 2013Review
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5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundRecent studies of Haloferax volcanii have begun to elucidate the steps of N-glycosylation in Archaea, where this universal post-translational modification remains poorly described. In Hfx. volcanii, a series of Agl proteins catalyzes the assembly and attachment of a N-linked pentasaccharide to the S-layer glycoprotein. Although roles have been assigned to the majority of Agl proteins, others await description. In the following, the contribution of AglR to N-glycosylation was addressed.
methodsA combination of bioinformatics, gene deletion, mass spectrometry and metabolic radiolabeling served to show a role for AglR in archaeal N-glycosylation at both the dolichol phosphate and reporter glycoprotein levels.
resultsThe modified behavior of the S-layer glycoprotein isolated from cells lacking AglR points to an involvement of this protein in N-glycosylation. In cells lacking AglR, glycan-charged dolichol phosphate, including mannose-charged dolichol phosphate, accumulates. At the same time, the S-layer glycoprotein does not incorporate mannose, the final subunit of the N-linked pentasaccharide decorating this protein. AglR is a homologue of Wzx proteins, annotated as flippases responsible for delivering lipid-linked O-antigen precursor oligosaccharides across the bacterial plasma membrane during lipopolysaccharide biogenesis.
conclusionsThe effects resulting from aglR deletion are consistent with AglR interacting with dolichol phosphate-mannose, possibly acting as a dolichol phosphate-mannose flippase or contributing to such activity. GENERAL SIGNIFICANCE: Little is known of how lipid-linked oligosaccharides are translocated across membrane during N-glycosylation. The possibility of Hfx. volcanii AglR mediating or contributing to flippase activity could help address this situation.
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