Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9139932 | Molecular and Biochemical Parasitology | 2005 | 6 Pages |
Abstract
N-linked glycosylation is the most frequent modification of secretory proteins. The central reaction of this process in eukaryotic cells is catalyzed by the hetero-oligomeric protein complex oligosaccharyltransferase (OST). The gene STT3 gene encodes a protein, which is the most conserved among the components of the OST. In this report, we describe the isolation and functional characterization of a STT3 homologue from Toxoplasma gondii. The topology of the TgStt3p is similar to that of the yeast Stt3p with 47% identity. We demonstrate that high level expression of the homologues gene is required to completely suppress the defect caused by a stt3 mutation in yeast, suggesting that homologous Stt3 proteins can serve analogous functions in distantly related eukaryotic cells regardless of their degree of conservation.
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Authors
Hosam Shams-Eldin, Thomas Blaschke, Darisuren Anhlan, Sebastian Niehus, Jan Müller, Nahid Azzouz, Ralph T. Schwarz,