Protein glycosylation in Haloferax volcanii: partial characterization of a 98-kDa glycoprotein.

Abstract

The plasma membrane of Haloferax volcanii contains several glycoproteins, including a 98-kDa species. Using lectin-based chromatography, the glycoprotein was isolated and partially characterized. Sequence comparison, based on antibody binding as well as one-dimensional peptide maps show that the 98-kDa glycoprotein is distinct from the S-layer glycoprotein, the major glycoprotein in H. volcanii. The 98-kDa glycoprotein can be further distinguished from the S-layer glycoprotein on the basis of membrane attachment. Unlike the S-layer glycoprotein, the 98-kDa glycoprotein is not associated with the membrane in a Mg2+-dependent manner. Both proteins, however, apparently rely on a similar mechanism of glycosylation, since neither was affected by treatment with bacitracin or tunicamycin, agents known to interfere with protein glycosylation in other species. Finally, the pattern of glycosylation of the 98-kDa glycoprotein is not shared by a 95-kDa glycoprotein of the related Haloferax mediterranei strain.