ArticleJournal of bacteriology2008
Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- 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
- Article
- AglM and VNG1048G, Two Haloarchaeal UDP-Glucose Dehydrogenases, Show Different Salt-Related Behaviors.Life (Basel, Switzerland) · 2016Article
- Article
- 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
- Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.Applied and environmental microbiology · 2014Article
- Haloferax volcanii N-glycosylation: delineating the pathway of dTDP-rhamnose biosynthesis.PloS one · 2014Article
- N-glycosylation in Haloferax volcanii: adjusting the sweetness.Frontiers in microbiology · 2013Article
- Article
- Article
- AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase.Journal of bacteriology · 2012Article
- N-glycosylation of Haloferax volcanii flagellins requires known Agl proteins and is essential for biosynthesis of stable flagella.Journal of bacteriology · 2012Article
- Glyco-engineering in Archaea: differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain.Microbial biotechnology · 2011Article
- Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein.Molecular microbiology · 2010Article
- Towards glycoengineering in archaea: replacement of Haloferax volcanii AglD with homologous glycosyltransferases from other halophilic archaea.Applied and environmental microbiology · 2010Article
- Identification of residues important for the activity of Haloferax volcanii AglD, a component of the archaeal N-glycosylation pathway.Archaea (Vancouver, B.C.) · 2010Article
- Biosynthesis and role of N-linked glycosylation in cell surface structures of archaea with a focus on flagella and s layers.International journal of microbiology · 2010Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Eukarya, N glycosylation involves the actions of enzymes working on both faces of the endoplasmic reticulum membrane. The steps of bacterial N glycosylation, in contrast, transpire essentially on the cytoplasmic side of the plasma membrane, with only transfer of the assembled glycan to the target protein occurring on the external surface of the cell. For Archaea, virtually nothing is known about the topology of enzymes involved in assembling those glycans that are subsequently N linked to target proteins on the external surface of the cell. To remedy this situation, subcellular localization and topology predictive algorithms, protease accessibility, and immunoblotting, together with cysteine modification following site-directed mutagenesis, were enlisted to define the topology of Haloferax volcanii proteins experimentally proven to participate in the N-glycosylation process. AglJ and AglD, involved in the earliest and latest stages, respectively, of assembly of the pentasaccharide decorating the H. volcanii S-layer glycoprotein, were shown to present their soluble N-terminal domain, likely containing the putative catalytic site of each enzyme, to the cytosol. The same holds true for Alg5-B, Dpm1-A, and Mpg1-D, proteins putatively involved in this posttranslational event. The results thus point to the assembly of the pentasaccharide linked to certain Asn residues of the H. volcanii S-layer glycoprotein as occurring within the cell.
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