TheSchizosaccharomyces pombe gms1+Gene Encodes an UDP-Galactose Transporter Homologue Required for Protein Galactosylation

Tabuchi, Mitsuaki; Tanaka, Naotaka; Iwahara, Shojiro; Takegawa, Kaoru

doi:10.1006/bbrc.1997.6239

Cited by 72 publications

(74 citation statements)

References 22 publications

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“…We previously reported that disruption of the gms1 + gene led to a complete loss of protein galactosylation, due to a defect in transport of UDPgalactose from the cytosol to the lumen of the Golgi apparatus as a substrate for galactosyltransferase ( Fig. 7) (Tabuchi et al, 1997;. The gms1D strain exhibited aberrant cell morphology and increased sensitivity to digestion with b-glucanase and to various drugs, such as hygromycin B, sodium orthovanadate and calcofluor white.…”

Section: Discussionmentioning

confidence: 96%

“…The galactose residues are modified by galactosyltransferases using UDPgalactose as substrate (Andreishcheva et al, 2004; Chappell et al, 1994;Yoko-o et al, 1998). UDP-galactose is transported to the Golgi lumen from the cytosol by a Golgi-localized UDP-galactose transporter (Gms1p) (Tabuchi et al, 1997;). In Sch.…”

Section: Discussionmentioning

confidence: 99%

“…pombe strain ARC039 (h 2 leu1-32 ura4-C190T) was used. The gms1D strain was constructed as described by Tabuchi et al (1997). Standard rich medium (YES) and synthetic minimal medium (MM) for growing Sch.…”

Section: Methodsmentioning

confidence: 99%

“…It is interesting to note that only Schizosaccharomyces species have two types of UDPglucose/-galactose 4-epimerase, while other yeast species have only the Sc Gal10 type (epimerase and mutarotase domains). This might be related to the fact that unlike other yeast species, Schizosaccharomyces species secrete galactomannoproteins and possess galactosylation mechanisms mediated by galactosyltransferases, and have UDPgalactose transporters (Chappell et al, 1994;Ohashi et al, 2009;Tabuchi et al, 1997;Umeda et al, 2000). Therefore, like mammalian cells, Schizosaccharomyces species must produce UDP-galactose constitutively from UDP-glucose via UDP-glucose/-galactose 4-epimerase as a substrate for galactosyltransferases and UDP-galactose transporters.…”

Section: Sch Pombe Has Two Types Of Udp-glucose/ -Galactose 4-epimerasementioning

confidence: 99%

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Characterization of two different types of UDP-glucose/-galactose4-epimerase involved in galactosylation in fission yeast

et al. 2010

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Schizosaccharomyces species are currently the only known organisms with two types of genes encoding UDP-glucose/-galactose 4-epimerase, uge1 + and gal10 + . A strain deleted for uge1 + exhibited a severe galactosylation defect and a decrease in activity and in UDP-galactose content when grown in glucose-rich medium (2 % glucose), indicating that Uge1p is a major UDPglucose/-galactose 4-epimerase under these growth conditions. In contrast, gal10 + was efficiently expressed and involved in galactosylation of cell-surface proteins in low-glucose medium (0.1 % glucose and 2 % glycerol), but not in galactose-containing medium. In a uge1Dgal10D strain, the galactosylation defect was suppressed and UDP-galactose content restored to wild-type levels in galactose-containing medium. Disruption of gal7 + , encoding galactose-1-phosphate uridylyltransferase, in the uge1Dgal10D strain reversed suppression of the galactosylation defect and reduced levels of UDP-galactose, indicating that galactose is transported from the medium to the cytosol and is converted into UDP-galactose via galactose 1-phosphate by Gal7p in Sch. pombe. INTRODUCTIONGlycoproteins in the fission yeast Schizosaccharomyces pombe contain a large amount of galactose in addition to both N-and O-linked mannan (Manners & Meyer, 1977;Moreno et al., 1985;Ikeda et al., 2009;Ohashi et al., 2009), indicating that Sch. pombe is equipped with mechanisms for glycoprotein galactosylation like animal cells. Research has demonstrated that the outer chain structure of galactomannan has an a-1,2-linked galactose or pyruvylated galactose attached to a poly-a-1,6-linked mannose backbone (Gemmill & Trimble, 1998), and that the pyruvylated galactose epitope bears remarkable structural resemblance to the N-acetylneuraminic acid-linked galactose epitope found in mammalian cells (Gemmill & Trimble, 1996). These galactose residues are enzymically modified by galactosyltransferases using UDP-galactose as substrate (Andreishcheva et al., 2004; Chappell et al., 1994;Yoko-o et al., 1998). UDP-galactose is transported to the Golgi lumen from the cytosol by the Golgi-localized UDPgalactose transporter (Gms1p) (Tabuchi et al., 1997;). In Sch. pombe, the precise manner in which UDP-galactose is synthesized in the cytosol has been unclear. In the cytosol, the key enzyme for UDP-galactose synthesis is UDP-galactose/-glucose 4-epimerase, which catalyses the interconversion of UDPgalactose and UDP-D-glucose. Interestingly, Schizosaccharomyces species have two types of UDP-glucose/-galactose 4-epimerase, while other organisms have only one. It is not known why two types of epimerase are needed and how they are regulated in Sch. pombe.In Saccharomyces cerevisiae, Gal10p is the sole UDPglucose/-galactose 4-epimerase, which consists of a UDPglucose/-galactose 4-epimerase domain and a galactose mutarotase domain (Majumdar et al., 2004;Scott & Timson, 2007;Thoden & Holden, 2005), and which catalyses mutarotation of a-galactose to b-galactose. Expression of the GAL10 gene is regulated by Gal4p, a DNA...

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Sch Pombe Has Two Types Of Udp-glucose/ -Galactose 4-epimerasementioning

confidence: 99%

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Characterization of two different types of UDP-glucose/-galactose4-epimerase involved in galactosylation in fission yeast

et al. 2010

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“…4b). To further analyse the localization of Vsl1p, we co-expressed GFP-Vsl1p and RFP-fused Gms1p, which is a UDP-Gal transporter and is used as a Golgi marker protein (Tabuchi et al, 1997b;Nakase et al, 2010), and revealed that GFP-Vsl1p was not co-localized with Gms1p-RFP (Fig. 4c).…”

Section: Vsl1p Is Localized To the Vacuolar Membrane And Prevacuolar mentioning

confidence: 99%

Vsl1p cooperates with Fsv1p for vacuolar protein transport and homotypic fusion in Schizosaccharomyces pombe

et al. 2015

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Members of the SNARE protein family participate in the docking-fusion step of several intracellular vesicular transport events. Saccharomyces cerevisiae Vam7p was identified as a SNARE protein that acts in vacuolar protein transport and membrane fusion. However, in Schizosaccharomyces pombe, there have been no reports regarding the counterpart of Vam7p. Here, we found that, although the SPCC594.06c gene has low similarity to Vam7p, the product of SPCC594.06c has a PX domain and SNARE motif like Vam7p, and thus we designated the gene Sch. pombe vsl1 + (Vam7-like protein 1). The vsl1D cells showed no obvious defect in vacuolar protein transport. However, cells of the vsl1D mutant with a deletion of fsv1 + , which encodes another SNARE protein, displayed extreme defects in vacuolar protein transport and vacuolar morphology. Vsl1p was localized to the vacuolar membrane and prevacuolar compartment, and its PX domain was essential for proper localization. Expression of the fusion protein GFP-Vsl1p was able to suppress ZnCl 2 sensitivity and the vacuolar protein sorting defect in the fsv1D cells. Moreover, GFP-Vsl1p was mislocalized in a pep12D mutant and in cells overexpressing fsv1 + . Importantly, overexpression of Sac. cerevisiae VAM7 could suppress the sensitivity to ZnCl 2 of vsl1D cells and the vacuolar morphology defect of vsl1Dfsv1D cells in Sch. pombe. Taken together, these data suggest that Vsl1p and Fsv1p are required for vacuolar protein transport and membrane fusion, and they function cooperatively with Pep12p in the same membrane-trafficking step.

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Schizosaccharomyces pombegmd3+/alg11+ is a functional homologue ofSaccharomyces cerevisiaeALG11 which is involved inN-linked oligosaccharide synthesis

Umeda

Yoko-o

Nakayama

et al. 2000

Yeast

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The oligosaccharide of glycoproteins in the ®ssion yeast Schizosaccharomyces pombe is unique in containing galactose. We isolated four mutants that had reduced amounts of galactose residues on their cell surface glycoproteins by ¯uorescence-activated cell sorter. The isolated four recessive mutants, gmd1 to gmd4, showed a defect in glycosylation of acid phosphatase, a cell surface glycoprotein. In gmd3 mutant cells, the amounts of both mannose and galactose residues were decreased on the cell surface galactomannoproteins, suggesting an underglycosylation of galactomannoproteins. The gmd3 + gene encodes a protein that has signi®cant similarity with Saccharomyces cerevisiae Alg11p and is likely to be involved in N-linked core oligosaccharide synthesis. ALG11 suppressed the gmd3 mutation, indicating that gmd3 + gene is a functional homologue of the ALG11 gene. We therefore designated gmd3 + as alg11 + .

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TheSchizosaccharomyces pombe gms1+Gene Encodes an UDP-Galactose Transporter Homologue Required for Protein Galactosylation

Cited by 72 publications

References 22 publications

Characterization of two different types of UDP-glucose/-galactose4-epimerase involved in galactosylation in fission yeast

Characterization of two different types of UDP-glucose/-galactose4-epimerase involved in galactosylation in fission yeast

Vsl1p cooperates with Fsv1p for vacuolar protein transport and homotypic fusion in Schizosaccharomyces pombe

Schizosaccharomyces pombegmd3+/alg11+ is a functional homologue ofSaccharomyces cerevisiaeALG11 which is involved inN-linked oligosaccharide synthesis

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