High impact information on gms1

• We isolated a mutant (gms1) that is deficient in galactosylation of cell surface glycoproteins in Sz.pombe, and found that the gms1(+) gene encodes a UDP-galactose transporter [1].
• We previously found that the disruption of gms1+, a gene encoding the UDP-galactose transporter required for the synthesis of galactomannan, led to the complete defect of cell surface galactosylation in Sz. pombe [2].
• The deletion strain of gms1+ was viable; however, itshowed an aberrant cell morphology and increased sensitivities to digestion with beta-glucanase and to various drugs, such as hygromycin B, sodium orthovanadate and Calcofluor white [2].
• 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 [3].
• From an S. pombe genomic library, we cloned the gms1+ gene which restored the galactosylation of cell wall glycoproteins [3].

Associations of gms1 with chemical compounds

• Structural studies on N-linked oligosaccharides from gms1 mutant cells showed that the number of alpha-1,2-linked galactose residues wes markedly reduced, and unsubstituted alpha-1,6-linked polymannose outer chains were attached to the core oligosaccharides [4].

Analytical, diagnostic and therapeutic context of gms1

• The Schizosaccharomyces pombe UDP-galactose transporter cDNA (SpUGT cDNA), encoding the product of the gms1+ gene which consists of two exon sequences separated by a 173-bp intron, was cloned by RT-PCR [5].

References