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J Biol Chem, Vol. 273, Issue 41, 26836-26843, October 9, 1998
From the Medical Research Council Laboratory of Molecular Biology,
Hills Road, Cambridge CB2 2QH, United Kingdom
The mannan structure found on the
N-linked glycans of the yeast Saccharomyces
cerevisiae is composed of a long backbone of 
-1,6-linked
mannose to which are attached branches consisting of two -1,2-linked
mannoses followed by an -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 -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
-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.
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