Rayner JC, Munro S Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae Journal of Biological Chemistry273(41) (1998)
26836-26843
/Variants 0/-+
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-6)-a-D-Manp-(1-
/Variants 0/ is:
a-D-Manp-(1-2)-
OR (exclusively)
a-D-Manp-(1-2)-a-D-Manp-(1-2)-
OR (exclusively)
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-
OR (exclusively)
a-D-Manp-(1-3)-a-D-Manp-(1-2)-+
|
a-D-Manp-(1-3)-a-D-Manp-(1--P--6)--a-D-Manp-(1-2)-
NCBI PubMed ID:9756928 Publication DOI:10.1074/jbc.273.41.26836 Journal NLM ID:2985121R Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology Correspondence: Munro S <seanmrc-lmb.cam.ac.uk> Institutions: Medical Research Council Laboratory of Molecular Biology, Cambridge, UK
The mannan structure found on the N-linked glycans of the yeast Saccharomyces cerevisiae is composed of a long backbone of α-1,6-linked mannose to which are attached branches consisting of two α-1,2-linked mannoses followed by an α-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 α-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 α- 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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