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AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.

Publication ,  Journal Article
Kaminski, L; Abu-Qarn, M; Guan, Z; Naparstek, S; Ventura, VV; Raetz, CRH; Hitchen, PG; Dell, A; Eichler, J
Published in: J Bacteriol
November 2010

Like the Eukarya and Bacteria, the Archaea also perform N glycosylation. Using the haloarchaeon Haloferax volcanii as a model system, a series of Agl proteins involved in the archaeal version of this posttranslational modification has been identified. In the present study, the participation of HVO_1517 in N glycosylation was considered, given its homology to a known component of the eukaryal N-glycosylation pathway and because of the genomic proximity of HVO_1517 to agl genes encoding known elements of the H. volcanii N-glycosylation process. By combining the deletion of HVO_1517 with mass spectrometric analysis of both dolichol phosphate monosaccharide-charged carriers and the S-layer glycoprotein, evidence was obtained showing the participation of HVO_1517, renamed AglJ, in adding the first hexose of the N-linked pentasaccharide decorating this reporter glycoprotein. The deletion of aglJ, however, did not fully prevent the attachment of a hexose residue to the S-layer glycoprotein. Moreover, in the absence of AglJ, the level of only one of the three monosaccharide-charged dolichol phosphate carriers detected in the cell was reduced. Nonetheless, in cells lacking AglJ, no further sugar subunits were added to the remaining monosaccharide-charged dolichol phosphate carriers or to the monosaccharide-modified S-layer glycoprotein, pointing to the importance of the sugar added through the actions of AglJ for proper N glycosylation. Finally, while aglJ can be deleted, H. volcanii surface layer integrity is compromised in the absence of the encoded protein.

Duke Scholars

Published In

J Bacteriol

DOI

EISSN

1098-5530

Publication Date

November 2010

Volume

192

Issue

21

Start / End Page

5572 / 5579

Location

United States

Related Subject Headings

  • Molecular Structure
  • Molecular Sequence Data
  • Microbiology
  • Membrane Glycoproteins
  • Hexoses
  • Haloferax volcanii
  • Glycosylation
  • Gene Expression Regulation, Archaeal
  • Gene Deletion
  • Carrier Proteins
 

Citation

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Kaminski, L., Abu-Qarn, M., Guan, Z., Naparstek, S., Ventura, V. V., Raetz, C. R. H., … Eichler, J. (2010). AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. J Bacteriol, 192(21), 5572–5579. https://doi.org/10.1128/JB.00705-10
Kaminski, Lina, Mehtap Abu-Qarn, Ziqiang Guan, Shai Naparstek, Valeria V. Ventura, Christian R. H. Raetz, Paul G. Hitchen, Anne Dell, and Jerry Eichler. “AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.J Bacteriol 192, no. 21 (November 2010): 5572–79. https://doi.org/10.1128/JB.00705-10.
Kaminski L, Abu-Qarn M, Guan Z, Naparstek S, Ventura VV, Raetz CRH, et al. AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. J Bacteriol. 2010 Nov;192(21):5572–9.
Kaminski, Lina, et al. “AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein.J Bacteriol, vol. 192, no. 21, Nov. 2010, pp. 5572–79. Pubmed, doi:10.1128/JB.00705-10.
Kaminski L, Abu-Qarn M, Guan Z, Naparstek S, Ventura VV, Raetz CRH, Hitchen PG, Dell A, Eichler J. AglJ adds the first sugar of the N-linked pentasaccharide decorating the Haloferax volcanii S-layer glycoprotein. J Bacteriol. 2010 Nov;192(21):5572–5579.

Published In

J Bacteriol

DOI

EISSN

1098-5530

Publication Date

November 2010

Volume

192

Issue

21

Start / End Page

5572 / 5579

Location

United States

Related Subject Headings

  • Molecular Structure
  • Molecular Sequence Data
  • Microbiology
  • Membrane Glycoproteins
  • Hexoses
  • Haloferax volcanii
  • Glycosylation
  • Gene Expression Regulation, Archaeal
  • Gene Deletion
  • Carrier Proteins