ArticleEnvironmental microbiology2012
Protein glycosylation as an adaptive response in Archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation.
Article in Environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 90 citations in OpenAlex.
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- Osmoregulation in freshwater anaerobic methane-oxidizing archaea under salt stress.The ISME journal · 2024Article
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- Functional Insights of Salinity Stress-Related Pathways in Metagenome-ResolvedApplied and environmental microbiology · 2022Article
- An archaeal histone-like protein regulates gene expression in response to salt stress.Nucleic acids research · 2021Article
- Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea.PLoS biology · 2021Article
- The Polygonal Cell Shape and Surface Protein Layer of Anaerobic Methane-OxidizingFrontiers in microbiology · 2021Article
- Insights into gene expression changes under conditions that facilitate horizontal gene transfer (mating) of a model archaeon.Scientific reports · 2020Article
- Identification of a novelThe Journal of biological chemistry · 2020Article
- Interaction of two strongly divergent archaellins stabilizes the structure of the Halorubrum archaellum.MicrobiologyOpen · 2020Article
- Improved Isolation of SlaA and SlaB S-layer proteins in Sulfolobus acidocaldarius.Extremophiles : life under extreme conditions · 2020Article
- The Archaeal Proteome Project advances knowledge about archaeal cell biology through comprehensive proteomics.Nature communications · 2020Article
- Species-Specific Recognition ofmBio · 2020Article
- Analysis of Cell-Cell Bridges inFrontiers in microbiology · 2020Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
To cope with life in hypersaline environments, halophilic archaeal proteins are enriched in acidic amino acids. This strategy does not, however, offer a response to transient changes in salinity, as would post-translational modifications. To test this hypothesis, N-glycosylation of the Haloferax volcanii S-layer glycoprotein was compared in cells grown in high (3.4 M NaCl) and low (1.75 M NaCl) salt, as was the glycan bound to dolichol phosphate, the lipid upon which the N-linked glycan is assembled. In high salt, S-layer glycoprotein Asn-13 and Asn-83 are modified by a pentasaccharide, while dolichol phosphate is modified by a tetrasaccharide comprising the first four pentasaccharide residues. When the same targets were considered from cells grown in low salt, substantially less pentasaccharide was detected. At the same time, cells grown at low salinity contain dolichol phosphate modified by a distinct tetrasaccharide absent in cells grown at high salinity. The same tetrasaccharide modified S-layer glycoprotein Asn-498 in cells grown in low salt, whereas no glycan decorated this residue in cells grown in the high-salt medium. Thus, in response to changes in environmental salinity, Hfx. volcanii not only modulates the N-linked glycans decorating the S-layer glycoprotein but also the sites of such post-translational modification.
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