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AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.

Publication ,  Journal Article
Kaminski, L; Guan, Z; Abu-Qarn, M; Konrad, Z; Eichler, J
Published in: Biochim Biophys Acta
October 2012

BACKGROUND: Recent studies of Haloferax volcanii have begun to elucidate the steps of N-glycosylation in Archaea, where this universal post-translational modification remains poorly described. In Hfx. volcanii, a series of Agl proteins catalyzes the assembly and attachment of a N-linked pentasaccharide to the S-layer glycoprotein. Although roles have been assigned to the majority of Agl proteins, others await description. In the following, the contribution of AglR to N-glycosylation was addressed. METHODS: A combination of bioinformatics, gene deletion, mass spectrometry and metabolic radiolabeling served to show a role for AglR in archaeal N-glycosylation at both the dolichol phosphate and reporter glycoprotein levels. RESULTS: The modified behavior of the S-layer glycoprotein isolated from cells lacking AglR points to an involvement of this protein in N-glycosylation. In cells lacking AglR, glycan-charged dolichol phosphate, including mannose-charged dolichol phosphate, accumulates. At the same time, the S-layer glycoprotein does not incorporate mannose, the final subunit of the N-linked pentasaccharide decorating this protein. AglR is a homologue of Wzx proteins, annotated as flippases responsible for delivering lipid-linked O-antigen precursor oligosaccharides across the bacterial plasma membrane during lipopolysaccharide biogenesis. CONCLUSIONS: The effects resulting from aglR deletion are consistent with AglR interacting with dolichol phosphate-mannose, possibly acting as a dolichol phosphate-mannose flippase or contributing to such activity. GENERAL SIGNIFICANCE: Little is known of how lipid-linked oligosaccharides are translocated across membrane during N-glycosylation. The possibility of Hfx. volcanii AglR mediating or contributing to flippase activity could help address this situation.

Duke Scholars

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

October 2012

Volume

1820

Issue

10

Start / End Page

1664 / 1670

Location

Netherlands

Related Subject Headings

  • Tandem Mass Spectrometry
  • Spectrometry, Mass, Electrospray Ionization
  • Protein Processing, Post-Translational
  • Polysaccharides
  • Organisms, Genetically Modified
  • Membrane Glycoproteins
  • Mannose
  • Haloferax volcanii
  • Glycosylation
  • Chromatography, Liquid
 

Citation

APA
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ICMJE
MLA
NLM
Kaminski, L., Guan, Z., Abu-Qarn, M., Konrad, Z., & Eichler, J. (2012). AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein. Biochim Biophys Acta, 1820(10), 1664–1670. https://doi.org/10.1016/j.bbagen.2012.06.014
Kaminski, Lina, Ziqiang Guan, Mehtap Abu-Qarn, Zvia Konrad, and Jerry Eichler. “AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.Biochim Biophys Acta 1820, no. 10 (October 2012): 1664–70. https://doi.org/10.1016/j.bbagen.2012.06.014.
Kaminski L, Guan Z, Abu-Qarn M, Konrad Z, Eichler J. AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein. Biochim Biophys Acta. 2012 Oct;1820(10):1664–70.
Kaminski, Lina, et al. “AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein.Biochim Biophys Acta, vol. 1820, no. 10, Oct. 2012, pp. 1664–70. Pubmed, doi:10.1016/j.bbagen.2012.06.014.
Kaminski L, Guan Z, Abu-Qarn M, Konrad Z, Eichler J. AglR is required for addition of the final mannose residue of the N-linked glycan decorating the Haloferax volcanii S-layer glycoprotein. Biochim Biophys Acta. 2012 Oct;1820(10):1664–1670.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

October 2012

Volume

1820

Issue

10

Start / End Page

1664 / 1670

Location

Netherlands

Related Subject Headings

  • Tandem Mass Spectrometry
  • Spectrometry, Mass, Electrospray Ionization
  • Protein Processing, Post-Translational
  • Polysaccharides
  • Organisms, Genetically Modified
  • Membrane Glycoproteins
  • Mannose
  • Haloferax volcanii
  • Glycosylation
  • Chromatography, Liquid