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Glycobiology vol 2 no 4 pp. 369-372, 1992
© 1992

research-article

Topology of ER processing {alpha}-mannosidase of Saccharomyces cerevisae

Benoît Grondin and Annette Herscovics1

McGill Cancer Centre, McGill University 3655 Drummond Street, Montreal, Quebec, H3G 1Y6, Canada

1To whom correspondence should be addressed

Received on April 5, 1992; accepted on May 13, 1992

The yeast specific {alpha}-mannosidase which converts Man9GlcNAc to a single isomer of Man8GlcNAc is involved in N-linked oligosaccharide processing in the endoplasmic reticulum (ER). Sequence analysis of the structural gene for this enzyme suggested that it is a type II transmembrane protein (Camirand et al., 1991). To firmly establish its membrane topology, the gene was transcribed in vitro and translation was performed in a reticulocyte lysate with and without dog pancreas microsomal membranes. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of [35S] products showed that the largest band formed corresponded in size to the 63 kDa peptide expected from the {alpha}-mannosidase gene product. It was transformed into a 4 kDa larger endoglycosidase H-sensitive band in the presence of microsomal membranes. This glycosylated translation product was completely protected from proteinase K digestion in the absence of detergent. These results demonstrate that the yeast ER {alpha}-mannosidase is a type II membrane protein, like Golgi enzymes involved in N-linked glycosylation.

endoplasmic reticulum retention topology transmembrane protein


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