The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation

In a previous study, we isolated a Schizosaccharomyces pombe mutant defective in protein galactosylation (Takegawa, K., Tanaka, N., Tabuchi, M. and Iwahara, S. (1996) Biosci. Biochem. Biotech. 60, 1156-1159). From an S. pombe genomic library, we cloned the gms1+ gene which restored the galactosylati...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-03, Vol.232 (1), p.121-125
Main Authors: Tabuchi, M, Tanaka, N, Iwahara, S, Takegawa, K
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological Transport
DNA, Recombinant
Genes, Fungal
Golgi Apparatus - metabolism
Humans
Molecular Sequence Data
Monosaccharide Transport Proteins - genetics
Monosaccharide Transport Proteins - metabolism
Schizosaccharomyces - genetics
Sequence Homology, Amino Acid
Uridine Diphosphate Galactose - metabolism
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Summary:In a previous study, we isolated a Schizosaccharomyces pombe mutant defective in protein galactosylation (Takegawa, K., Tanaka, N., Tabuchi, M. and Iwahara, S. (1996) Biosci. Biochem. Biotech. 60, 1156-1159). From an S. pombe genomic library, we cloned the gms1+ gene which restored the galactosylation of cell wall glycoproteins. Gms1 protein shares significant sequence similarity with human UDP-galactose and murine CMP-sialic acid transporters. The fission yeast strains deleted for the gms1+ gene lacked galactose residues in sell surface glycoproteins and were significantly decreased in UDP-galactose transport activity. These results showed that the gms1+ encodes an UDP-galactose transporter, and this protein appears to be an essential role for the incorporation of UDP-galactose into the lumen of Golgi in s. pombe.
ISSN:0006-291X
DOI:10.1006/bbrc.1997.6239