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J Biol Chem. 1984 Mar 25;259(6):3805-11.

Carbohydrate structure of Saccharomyces cerevisiae mnn9 mannoprotein.


The neutral oligosaccharides from Saccharomyces cerevisiae mnn1 mnn9, mnn2 mnn9, and mnn9 mutant mannoproteins, and from mnn1 and wild type carboxypeptidase Y, have been characterized. The major oligosaccharide from the mnn1 mnn9 mutant, Man10GlcNAc, has the structure (formula; see text) whereas the largest oligosaccharide from the mnn9 mutant, Man13GlcNAc, has the structure (formula; see text) the differences being due to the mnn1 mutation. The smaller mnn9 homologs had lesser amounts of terminal alpha 1----3-linked mannose and may be precursors of the mature oligosaccharide. The mnn2 mutation had no effect on the mnn9 oligosaccharide structures. Carboxypeptidase Y and mnn9 oligosaccharides were identical, which suggests that the mnn9 mutation eliminates the differences in carbohydrate structure that distinguish intra- from extracellular mannoproteins. One mnn1 mnn9 oligosaccharide, Man11GlcNAc, retained the terminal alpha 1----2-linked mannose of the lipid-linked core precursor, which suggests that processing to give the larger oligosaccharides can occur without removal of this unit. A smaller mnn1 mnn9 oligosaccharide, Man9GlcNAc, was a mixture of isomers that must, in part, have arisen by action of an alpha 1----2-mannosidase.

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