ArticleMicrobiologyOpen2015
Deciphering a pathway of Halobacterium salinarum N-glycosylation.
Article in MicrobiologyOpen, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Identification of the D-glucuronyl C5-epimerase that introduces iduronic acid into N-linked glycans decorating archaeal glycoproteins.Communications biology · 2025Article
- Article
- Agl28 and Agl29 are key components of a Halobacterium salinarum N-glycosylation pathway.FEMS microbiology letters · 2023Article
- Revisiting N-glycosylation in Halobacterium salinarum: Characterizing a dolichol phosphate- and glycoprotein-bound tetrasaccharide.Glycobiology · 2021Article
- Identifying Components of aFrontiers in microbiology · 2021Article
- Whole-genome comparison between the type strain of Halobacterium salinarum (DSM 3754MicrobiologyOpen · 2020Article
- Article
- Sialic Acid-Like Sugars in Archaea: Legionaminic Acid Biosynthesis in the HalophileFrontiers in microbiology · 2018Article
- Stereochemical Divergence of Polyprenol Phosphate Glycosyltransferases.Trends in biochemical sciences · 2018Review
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- AglM and VNG1048G, Two Haloarchaeal UDP-Glucose Dehydrogenases, Show Different Salt-Related Behaviors.Life (Basel, Switzerland) · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genomic analysis points to N-glycosylation as being a common posttranslational modification in Archaea. To date, however, pathways of archaeal N-glycosylation have only been described for few species. With this in mind, the similarities of N-linked glycans decorating glycoproteins in the haloarchaea Haloferax volcanii and Halobacterium salinarum directed a series of bioinformatics, genetic, and biochemical experiments designed to describe that Hbt. salinarum pathway responsible for biogenesis of one of the two N-linked oligosaccharides described in this species. As in Hfx. volcanii, where agl (archaeal glycosylation) genes that encode proteins responsible for the assembly and attachment of a pentasaccharide to target protein Asn residues are clustered in the genome, Hbt. salinarum also contains a group of clustered homologous genes (VNG1048G-VNG1068G). Introduction of these Hbt. salinarum genes into Hfx. volcanii mutant strains deleted of the homologous sequence restored the lost activity. Moreover, transcription of the Hbt. salinarum genes in the native host, as well as in vitro biochemical confirmation of the predicted functions of several of the products of these genes provided further support for assignments made following bioinformatics and genetic experiments. Based on the results obtained in this study, the first description of an N-glycosylation pathway in Hbt. salinarum is offered.
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