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Glycobiology. 2005 Apr;15(4):361-7. Epub 2004 Dec 1.

The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.

Author information

1
Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology Zurich, ETH Hönggerberg, CH-8093 Zürich, Switzerland.

Erratum in

  • Glycobiology. 2005 May;15(5):13G.

Abstract

In the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes.

PMID:
15574802
DOI:
10.1093/glycob/cwi019
[Indexed for MEDLINE]

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