ArticleBiochimica et biophysica acta2012
A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Unraveling the multiplicity of geranylgeranyl reductases in Archaea: potential roles in saturation of terpenoids.Extremophiles : life under extreme conditions · 2024Review
- N-glycosylation in Archaea - Expanding the process, components and roles of a universal post-translational modification.BBA advances · 2024Article
- An automated workflow to screen alkene reductases using high-throughput thin layer chromatography.Biotechnology for biofuels · 2020Article
- Discovery of novel geranylgeranyl reductases and characterization of their substrate promiscuity.Biotechnology for biofuels · 2018Article
- Lipid sugar carriers at the extremes: The phosphodolichols Archaea use in N-glycosylation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Article
- N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014Review
- Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.Nature chemical biology · 2013Article
- AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.Biochimica et biophysica acta · 2012Article
- Overview of the genetic tools in the Archaea.Frontiers in microbiology · 2012Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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Abstract
In N-glycosylation in both Eukarya and Archaea, N-linked oligosaccharides are assembled on dolichol phosphate prior to transfer of the glycan to the protein target. However, whereas only the α-position isoprene subunit is saturated in eukaryal dolichol phosphate, both the α- and ω-position isoprene subunits are reduced in the archaeal lipid. The agents responsible for dolichol phosphate saturation remain largely unknown. The present study sought to identify dolichol phosphate reductases in the halophilic archaeon, Haloferax volcanii. Homology-based searches recognize HVO_1799 as a geranylgeranyl reductase. Mass spectrometry revealed that cells deleted of HVO_1799 fail to fully reduce the isoprene chains of H. volcanii membrane phospholipids and glycolipids. Likewise, the absence of HVO_1799 led to a loss of saturation of the ω-position isoprene subunit of C(55) and C(60) dolichol phosphate, with the effect of HVO_1799 deletion being more pronounced with C(60) dolichol phosphate than with C(55) dolichol phosphate. Glycosylation of dolichol phosphate in the deletion strain occurred preferentially on that version of the lipid saturated at both the α- and ω-position isoprene subunits.
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