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Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae.

The mannan structure found on the N-linked glycans of the yeast Saccharomyces cerevisiae is composed of a long backbone of alpha-1, 6-linked mannose to which are attached branches consisting of two alpha-1,2-linked mannoses followed by an alpha-1,3-linked mannose. In the mutants mnn2 and mnn5, the addition of the first and second of these two mannoses, respectively, is defective. In this paper, we report the identification of the genes corresponding to these mutations. The two genes encode closely related proteins with distant homology to the known Mnn1p alpha-1,3-mannosyltransferase. We show that these proteins are localized in an early compartment of the yeast Golgi and that they are not physically associated with each other or with the two protein complexes known to be involved in synthesizing the alpha-1,6-linked backbone. The identification of Mnn2p and Mnn5p allows us to assign Golgi proteins to all of the catalytic steps in S. cerevisiae mannan synthesis.

Pubmed ID: 9756928


  • Rayner JC
  • Munro S


The Journal of biological chemistry

Publication Data

October 9, 1998

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Carbohydrate Conformation
  • Glycosylation
  • Mannans
  • Mannosyltransferases
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Open Reading Frames
  • Saccharomyces cerevisiae
  • Sequence Deletion
  • Sequence Homology, Amino Acid