N-glycosylation in Archaea: On the coordinated actions of Haloferax volcanii AglF and AglM

Sophie Yurist-Doutsch, Hilla Magidovich, Valeria V. Ventura, Paul G. Hitchen, Anne Dell, Jerry Eichler

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


Like Eukarya and Bacteria, Archaea are also capable of performing N-glycosylation. In the halophilic archaeon Haloferax volcanii, N-glycosylation is mediated by the products of the agl gene cluster. In the present report, this gene cluster was expanded to include an additional sequence, aglM, shown to participate in the biosynthesis of hexuronic acids contained within a pentasaccharide decorating the S-layer glycoprotein, a reporter H. volcanii glycoprotein. In response to different growth conditions, changes in the transcription profile of aglM mirrored changes in the transcription profiles of aglF, aglG and aglI, genes encoding confirmed participants in the H. volcanii N-glycosylation pathway, thus offering support to the hypothesis that in H. volcanii, N-glycosylation serves an adaptive role. Following purification, biochemical analysis revealed AglM to function as a UDP-glucose dehydrogenase. In a scoupled reaction with AglF, a previously identified glucose-1-phosphate uridyltransferase, UDP-glucuronic acid was generated from glucose-1-phosphate and UTP in a NAD+-dependent manner. These experiments thus represent the first step towards in vitro reconstitution of the archaeal N-glycosylation process.

Original languageEnglish
Pages (from-to)1047-1058
Number of pages12
JournalMolecular Microbiology
Issue number4
StatePublished - 1 Feb 2010

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology


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