ArticleThe Biochemical journal2002
Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 61 citations in OpenAlex.
- Characterization of aliA and aliB deletion mutants reveals a dominant role of AliA in Haloferax volcanii lipoprotein lipidation.The Journal of biological chemistry · 2026Article
- Microbial hauberks: composition and function of surface layer proteins in gammaproteobacterial methanotrophs.Applied and environmental microbiology · 2025Article
- Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Proteolysis at the Archaeal Membrane: Advances on the Biological Function and Natural Targets of Membrane-Localized Proteases inFrontiers in microbiology · 2022Review
- Complete atomic structure of a native archaeal cell surface.Cell reports · 2021Article
- Molecular Logic of Prokaryotic Surface Layer Structures.Trends in microbiology · 2021Review
- Improved Isolation of SlaA and SlaB S-layer proteins in Sulfolobus acidocaldarius.Extremophiles : life under extreme conditions · 2020Article
- MYXO-CTERM sorting tag directs proteins to the cell surface via the type II secretion system.Molecular microbiology · 2020Article
- Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Archaeal S-Layers: Overview and Current State of the Art.Frontiers in microbiology · 2017Review
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Are There Rab GTPases in Archaea?Molecular biology and evolution · 2016Article
- Permuting the PGF Signature Motif Blocks both Archaeosortase-Dependent C-Terminal Cleavage and Prenyl Lipid Attachment for the Haloferax volcanii S-Layer Glycoprotein.Journal of bacteriology · 2015Article
- Archaeal membrane-associated proteases: insights on Haloferax volcanii and other haloarchaea.Frontiers in microbiology · 2015Review
- S-layers: principles and applications.FEMS microbiology reviews · 2014Article
- Archaeal S-layer glycoproteins: post-translational modification in the face of extremes.Frontiers in microbiology · 2014Article
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations.Biochimica et biophysica acta · 2013Article
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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
Once the newly synthesized surface (S)-layer glycoprotein of the halophilic archaeaon Haloferax volcanii has traversed the plasma membrane, the protein undergoes a membrane-related, Mg(2+)-dependent maturation event, revealed as an increase in the apparent molecular mass and hydrophobicity of the protein. To test whether lipid modification of the S-layer glycoprotein could explain these observations, H. volcanii cells were incubated with a radiolabelled precursor of isoprene, [(3)H]mevalonic acid. In Archaea, isoprenoids serve as the major hydrophobic component of archaeal membrane lipids and have been shown to modify other haloarchaeal S-layer glycoproteins, although little is known of the mechanism, site or purpose of such modification. In the present study we report that the H. volcanii S-layer glycoprotein is modified by a derivative of mevalonic acid and that maturation of the protein was prevented upon treatment with mevinolin (lovastatin), an inhibitor of mevalonic acid biosynthesis. These findings suggest that lipid modification of S-layer glycoproteins is a general property of halophilic archaea and, like S-layer glycoprotein glycosylation, lipid-modification of the S-layer glycoproteins takes place on the external cell surface, i.e. following protein translocation across the membrane.
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