Mnt2p and Mnt3p of Saccharomyces cerevisiae are members of the Mnn1p family of  -1,3-mannosyltransferases responsible for adding the terminal mannose residues of O-linked oligosaccharides

Pedro Romero(McGill University), Marc Lussier(McGill University), Steeve Véronneau(McGill University), A.-M. Sdicu(McGill University), Annetté Herscovics(McGill University Health Centre), Howard Bussey(McGill University)
Glycobiology
October 1, 1999
Cited by 59Open Access
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Abstract

The genome of Saccharomyces cerevisiae contains five genes that encode type II transmembrane proteins with significant amino acid similarity to the alpha-1,3-mannosyltransferase Mnn1p. The roles of the three genes most closely related to MNN1 were examined in mutants carrying single and multiple combinations of the disrupted genes. Paper chromatographic analysis of [2-3H]mannose-labeled O-linked oligosaccharides released by beta-elimination showed that the MNT2 (YGL257c) and MNT3 (YIL014w) genes in combination with MNN1 have overlapping roles in the addition of the fourth and fifth alpha-1,3-linked mannose residues to form Man4 and Man5 oligosaccharides whereas MNT4 (YNR059w) does not appear to be required for O-glycan synthesis.


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