N-Linked oligosaccharides were elongated by glycosylation with mannose and galactose residues in the secretory pathway of Schizosaccharomyces pombe. The wild-type S. pombe cells were agglutinated by the additions of not only concanavalin A lectin, which is specific for mannose residues, but also PNA (from Arachis hypogaea) and RCA (Ricinus communis) lectins, which are specific for terminal galactose residues. By PNA-binding selection, we isolated an S. pombe mutant defective in protein glycosylation. The mutant cells, named gms1, were not agglutinated by PNA or RCA. In contrast, agglutination of the gms1 cells by the addition of concanavalin A was markedly increased. Structural studies on N-linked oligosaccharides from gms1 mutant cells showed that the number of α-1, 2-linked galactose residues was markedly reduced, and unsubstituted α-1, 6-linked polymannose outer chains were attached to the core oligosaccharides.

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