Journal
CHEMISTRY & BIOLOGY
Volume 12, Issue 12, Pages 1311-1316Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2005.10.004
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Funding
- NIGMS NIH HHS [GM65699-03, R01 GM039334, F32 GM065699, R01 GM039334-16, GM039334-19] Funding Source: Medline
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The gram-negative bacterium Campylobacter jejuni has a general N-linked glycosylation pathway encoded by the pgl gene cluster. One of the proteins in this cluster, PgIB, is thought to be the oligosaccharyl transferase due to its significant homology to Stt3p, a subunit of the yeast oligosaccharyl transferase complex. PgIB has been shown to be involved in catalyzing the transfer of an undecaprenyl-linked heptasaccharide to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif. Using a synthetic disaccharide glycan donor (GaINAc-alpha l,3-bacillosamine-pyrophosphate-unclecaprenyl) and a peptide acceptor substrate (KD FNVSKA), we can observe the oligosaccharyl transferase activity of PgIB in vitro. Furthermore, the preparation of additional unclecaprenyl-linked glycan variants reveals the ability of PgIB to transfer a wide variety of saccharides. With the demonstration of PgIB activity in vitro, fundamental questions surrounding the mechanism of N-linked glycosylation can now be addressed.
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