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Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes required for complex glycosylation of secreted proteins

Yip, C.L., Welch, S.K., Klebl, F., Gilbert, T., Seidel, P., Grant, F.J., O'Hara, P.J., MacKay, V.L.
Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.7 pp. 2723-2727
Saccharomyces cerevisiae, structural genes, hexosyltransferases, proteins, nucleotide sequences, amino acid sequences, Golgi apparatus, endoplasmic reticulum, protein secretion
Proteins secreted by the yeast Saccharomyces cerevisiae are usually modified by the addition at asparagine-linked glycosylation sites of large heterogeneous mannan units that are highly immunogenic. Secreted proteins from mnn1 mnn9 mutant strains, in contrast, have homogeneous Man10GlcNAc2 oligosaccharides that lack the immunogenic alpha 1,3-mannose linkages. We have cloned and sequenced the MNN9 and MNN1 genes, both of which encode proteins with the characteristics of type II membrane proteins. Mnn9p is a membrane-associated protein with unknown function that is required for the addition of the long alpha 1,6-mannose backbone of the complex mannan, whereas Mnn1p is most likely the alpha 1,3-mannosyltransferase located in the Golgi apparatus.