title: AglS, a novel component of the Haloferax volcanii N-glycosylation pathway, is a dolichol phosphate-mannose mannosyltransferase.
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 surface (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.
authors.affiliation: Department of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel.
authors.forename: Chen
authors.initials: C
authors.lastname: Cohen-Rosenzweig
authors.forename: Sophie
authors.initials: S
authors.lastname: Yurist-Doutsch
authors.forename: Jerry
authors.initials: J
authors.lastname: Eichler
mesh_terms: D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism; D004287:Dolichol Monophosphate Mannose / Q000378:metabolism*; D017353:Gene Deletion; D006031:Glycosylation; D019622:Haloferax volcanii / Q000235:genetics* / Q000378:metabolism*; D008364:Mannosyltransferases / Q000235:genetics* / Q000378:metabolism
chemical_list: D019843:Archaeal Proteins; D004287:Dolichol Monophosphate Mannose; D008364:Mannosyltransferases