PMID:23086206

Citation	Cohen-Rosenzweig, C, Yurist-Doutsch, S and Eichler, J' (2012) AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase. J. Bacteriol. '
Abstract	In Haloferax volcanii, a series of Agl proteins mediates protein N-glycosylation. The genes encoding all but one of the Agl proteins are sequestered into a single gene island. The same region of the genome includes sequences also suspected but not yet verified as serving N-glycosylation roles, such as HVO_1526. In the following, HVO_1526, renamed AglS, is shown to be necessary for the addition of the final mannose subunit of the pentasaccharide N-linked to the S-layer glycoprotein, a convenient reporter of N-glycosylation in Hfx. volcanii. Relying on bioinformatics, topological analysis, gene deletion, mass spectrometry and biochemical assays, AglS was shown to act as a dolichol phosphate-mannose mannosyltransferase, mediating the transfer of mannose from dolichol phosphate to the tetrasaccharide corresponding to the first four subunits of the pentasaccharide N-linked to the S-layer glycoprotein.
Links	PubMed Online version:10.1128/JB.01716-12
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HALVD:AGLS		GO:0005886: plasma membrane	ECO:0000314:		C		Fig 1B. Sub-cellular fractionation shows plasma membrane localization	complete CACAO 5645
HALVD:AGLS		GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity	ECO:0000314:		F		Fig 4B&C, table 1	complete CACAO 5646
HALVD:AGLS	enables	GO:0004169: dolichyl-phosphate-mannose-protein mannosyltransferase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
HALVD:AGLS	part_of	GO:0005886: plasma membrane	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete

References

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