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J Biol Chem, Vol. 274, Issue 10, 6579-6585, March 5, 1999
From the Medical Research Council Laboratory of Molecular Biology,
Hills Road, Cambridge, CB2 2QH, United Kingdom
In the yeast Saccharomyces cerevisiae
many of the N-linked glycans on cell wall and periplasmic
proteins are modified by the addition of mannan, a large
mannose-containing polysaccharide. Mannan comprises a backbone of
approximately 50
The Saccharomyces cerevisiae Protein Mnn10p/Bed1p Is
a Subunit of a Golgi Mannosyltransferase Complex
-1,6-linked mannoses to which are attached many
branches consisting of -1,2-linked and -1,3-linked mannoses. The
initiation and subsequent elongation of the mannan backbone is
performed by two complexes of proteins in the cis Golgi. In
this study we show that the product of the MNN10/BED1 gene is a component of one of these
complexes, that which elongates the backbone. Analysis of interactions
between the proteins in this complex shows that Mnn10p, and four
previously characterized proteins (Anp1p, Mnn9p, Mnn11p, and Hoc1p) are
indeed all components of the same large structure. Deletion of either Mnn10p, or its homologue Mnn11p, results in defects in mannan synthesis
in vivo, and analysis of the enzymatic activity of the complexes isolated from mutant strains suggests that Mnn10p and Mnn11p
are responsible for the majority of the -1,6-polymerizing activity
of the complex.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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