Modifications of lysosomal enzymes in Dictyostelium discoideum.
This paper has two purposes. The first is to review the past studies on the structure, biosynthesis, and immunological properties of a class of glycoproteins, the lysosomal enzymes, in Dictyostelium discoideum. The second purpose is to present new data on the analysis of mutant strains altered in the biosynthesis of the lipid-linked precursor of N-linked oligosaccharides, and on the characterization of new carbohydrate antigenic determinants found on multiple proteins in Dictyostelium. We will also show how a combination of genetic, biochemical and immunochemical approaches have been used to unravel a portion of the glycosylation pathway in Dictyostelium. The long-term goal of these studies is to use Dictyostelium discoideum as a model system to understand the functions of a variety of glycoconjugates in a multicellular organism. The existence of a large number of mutant strains which are altered in a variety of cellular functions, development and the posttranslational modification of multiple proteins, offers a great opportunity to explore this area.
D000946:Antigens, Fungal / Q000032:analysis; D002240:Carbohydrate Sequence; D002451:Cell Compartmentation; D004023:Dictyostelium / Q000235:genetics / Q000378:metabolism*; D000939:Epitopes; D006023:Glycoproteins / Q000276:immunology / Q000378:metabolism*; D006031:Glycosylation; D008247:Lysosomes / Q000201:enzymology*; D009154:Mutation; D011499:Protein Processing, Post-Translational; D013431:Sulfates / Q000378:metabolism
D000946:Antigens, Fungal; D000939:Epitopes; D006023:Glycoproteins; D013431:Sulfates