Haloferax volcanii

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  Subject Areas on Research

  • A predicted geranylgeranyl reductase reduces the ω-position isoprene of dolichol phosphate in the halophilic archaeon, Haloferax volcanii. 
  • AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. 
  • AglQ is a novel component of the Haloferax volcanii N-glycosylation pathway. 
  • AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein. 
  • Assembling Glycan-Charged Dolichol Phosphates: Chemoenzymatic Synthesis of a Haloferax volcanii N-Glycosylation Pathway Intermediate. 
  • Different routes to the same ending: comparing the N-glycosylation processes of Haloferax volcanii and Haloarcula marismortui, two halophilic archaea from the Dead Sea. 
  • Distinct Regions of the Haloferax volcanii Dolichol Phosphate-Mannose Synthase AglD Mediate the Assembly and Subsequent Processing of the Lipid-Linked Mannose. 
  • Distinct glycan-charged phosphodolichol carriers are required for the assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer glycoprotein. 
  • Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid. 
  • Gene Expression of Haloferax volcanii on Intermediate and Abundant Sources of Fixed Nitrogen. 
  • GlpR Is a Direct Transcriptional Repressor of Fructose Metabolic Genes in Haloferax volcanii. 
  • Glyco-engineering in Archaea: differential N-glycosylation of the S-layer glycoprotein in a transformed Haloferax volcanii strain. 
  • Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations. 
  • Protein glycosylation as an adaptive response in Archaea: growth at different salt concentrations leads to alterations in Haloferax volcanii S-layer glycoprotein N-glycosylation. 
  • Revisiting N-glycosylation in Halobacterium salinarum: Characterizing a dolichol phosphate- and glycoprotein-bound tetrasaccharide. 
  • Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans. 
  • Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity. 
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  Keywords of People

  • Guan, Ziqiang, Research Professor in Biochemistry, Biochemistry