PubMed:9363442 JSON TXT

Annnotations TAB JSON ListView MergeView

Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":427,"end":434},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":1218,"end":1225},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T3","span":{"begin":1392,"end":1399},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":1698,"end":1705},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T5","span":{"begin":1778,"end":1785},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":427,"end":434},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1218,"end":1225},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1392,"end":1399},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1698,"end":1705},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1778,"end":1785},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":427,"end":434},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":1218,"end":1225},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T3","span":{"begin":1392,"end":1399},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":1698,"end":1705},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T5","span":{"begin":1778,"end":1785},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

sentences

GlycoBiology-GDGDB

{"project":"GlycoBiology-GDGDB","denotations":[{"id":"_T1","span":{"begin":1530,"end":1547},"obj":"http://acgg.asia/db/diseases/gdgdb?con_ui=CON00008"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GlycoBiology-PACDB

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":73,"end":97},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC297"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":1290,"end":1301},"obj":"http://www.uniprot.org/uniprot/Q05639"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":73,"end":86},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4895"},{"id":"T2","span":{"begin":73,"end":86},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4930"},{"id":"T3","span":{"begin":73,"end":86},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/36034"},{"id":"T4","span":{"begin":73,"end":86},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4891"},{"id":"T5","span":{"begin":271,"end":281},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/2759"},{"id":"T6","span":{"begin":740,"end":744},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T7","span":{"begin":740,"end":744},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T8","span":{"begin":1064,"end":1076},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1369269"},{"id":"T9","span":{"begin":1092,"end":1097},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/998453"},{"id":"T10","span":{"begin":1136,"end":1141},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T11","span":{"begin":1177,"end":1182},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/998453"},{"id":"T12","span":{"begin":1377,"end":1382},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T13","span":{"begin":1627,"end":1632},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/998453"},{"id":"T14","span":{"begin":1756,"end":1761},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T15","span":{"begin":1860,"end":1865},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/998453"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":46,"end":59},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":110,"end":119},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":756,"end":765},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T4","span":{"begin":649,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0034975"},{"id":"T5","span":{"begin":649,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0033579"},{"id":"T6","span":{"begin":649,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0070972"},{"id":"T7","span":{"begin":649,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0033577"},{"id":"T8","span":{"begin":649,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0035437"},{"id":"T9","span":{"begin":649,"end":678},"obj":"http://purl.obolibrary.org/obo/GO_0045047"},{"id":"T10","span":{"begin":740,"end":755},"obj":"http://purl.obolibrary.org/obo/GO_0006077"},{"id":"T11","span":{"begin":740,"end":765},"obj":"http://purl.obolibrary.org/obo/GO_0006078"},{"id":"T12","span":{"begin":740,"end":755},"obj":"http://purl.obolibrary.org/obo/GO_0006078"},{"id":"T13","span":{"begin":740,"end":755},"obj":"http://purl.obolibrary.org/obo/GO_0006079"},{"id":"T14","span":{"begin":749,"end":765},"obj":"http://purl.obolibrary.org/obo/GO_0009250"},{"id":"T15","span":{"begin":962,"end":984},"obj":"http://purl.obolibrary.org/obo/GO_0004573"},{"id":"T16","span":{"begin":1828,"end":1850},"obj":"http://purl.obolibrary.org/obo/GO_0004573"},{"id":"T17","span":{"begin":1077,"end":1084},"obj":"http://purl.obolibrary.org/obo/GO_0090485"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":459,"end":480},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T2","span":{"begin":649,"end":670},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T3","span":{"begin":730,"end":734},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":1136,"end":1141},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1377,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1756,"end":1761},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":730,"end":739},"obj":"http://purl.obolibrary.org/obo/GO_0005618"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

EDAM-topics

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":213,"end":220},"obj":"http://edamontology.org/data_1467"},{"id":"T2","span":{"begin":213,"end":220},"obj":"http://edamontology.org/format_1208"},{"id":"T3","span":{"begin":234,"end":241},"obj":"http://edamontology.org/operation_2409"},{"id":"T4","span":{"begin":234,"end":241},"obj":"http://edamontology.org/operation_0004"},{"id":"T5","span":{"begin":283,"end":293},"obj":"http://edamontology.org/operation_0004"},{"id":"T6","span":{"begin":283,"end":293},"obj":"http://edamontology.org/operation_2409"},{"id":"T7","span":{"begin":583,"end":593},"obj":"http://edamontology.org/data_0842"},{"id":"T8","span":{"begin":583,"end":593},"obj":"http://edamontology.org/data_2611"},{"id":"T9","span":{"begin":671,"end":678},"obj":"http://edamontology.org/format_1208"},{"id":"T10","span":{"begin":671,"end":678},"obj":"http://edamontology.org/data_1467"},{"id":"T11","span":{"begin":671,"end":700},"obj":"http://edamontology.org/data_0989"},{"id":"T12","span":{"begin":690,"end":700},"obj":"http://edamontology.org/data_0842"},{"id":"T13","span":{"begin":690,"end":700},"obj":"http://edamontology.org/data_2611"},{"id":"T14","span":{"begin":723,"end":729},"obj":"http://edamontology.org/operation_3435"},{"id":"T15","span":{"begin":949,"end":957},"obj":"http://edamontology.org/operation_2945"},{"id":"T16","span":{"begin":1226,"end":1234},"obj":"http://edamontology.org/data_1756"},{"id":"T17","span":{"begin":1401,"end":1409},"obj":"http://edamontology.org/operation_2945"},{"id":"T18","span":{"begin":1706,"end":1714},"obj":"http://edamontology.org/data_1756"},{"id":"T19","span":{"begin":1786,"end":1794},"obj":"http://edamontology.org/data_1756"},{"id":"T20","span":{"begin":1929,"end":1939},"obj":"http://edamontology.org/data_0883"},{"id":"T21","span":{"begin":1929,"end":1948},"obj":"http://edamontology.org/data_1070"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

GlyTouCan-IUPAC

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1365,"end":1373},"obj":"id"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":1456,"end":1463},"obj":"id"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":73,"end":97},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":271,"end":281},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":916,"end":921},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"4932"},{"id":"A2","pred":"db_id","subj":"T2","obj":"2759"},{"id":"A3","pred":"db_id","subj":"T3","obj":"9606"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":471,"end":480},"obj":"Body_part"},{"id":"T2","span":{"begin":661,"end":670},"obj":"Body_part"},{"id":"T3","span":{"begin":735,"end":739},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000060"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}

CL-cell

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":1092,"end":1097},"obj":"Cell"},{"id":"T2","span":{"begin":1177,"end":1182},"obj":"Cell"},{"id":"T3","span":{"begin":1627,"end":1632},"obj":"Cell"},{"id":"T4","span":{"begin":1860,"end":1865},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0004124"}],"text":"The yeast CWH41 gene encodes glucosidase I.\nN-Glycosylation in the yeast Saccharomyces cerevisiae entails the synthesis of a Glc3Man9GlcNAc2 oligosaccharide precursor which is subsequently transferred to suitable protein acceptors, a process which is conserved among all eukaryotes. Processing of the oligosaccharide occurs immediately following this transfer, the first step being the removal of the terminal alpha-1,2-linked glucose by glucosidase I in the endoplasmic reticulum. Although yeast glucosidase I has been isolated, the yeast gene encoding this enzyme has not yet been identified. In the present work, it is shown that Cwh41p, a yeast endoplasmic reticulum protein previously identified as being required for normal cell wall beta-1,6-glucan synthesis (Jiang, Sheraton, Ram, Dijkgraaf, Klis, and Bussey (1996) J. Bacteriol., 178, 1162-1171), has significant amino acid similarity to the product of the human glucosidase I cDNA. Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3. It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1--\u003e2 alpha-D-Glc 1--\u003e3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro. Following 1 h labeling of cells with [3H]mannose, analysis by high pressure liquid chromatography of the labeled N-linked oligosaccharides, combined with treatment with jack bean alpha mannosidase and yeast glucosidase I, shows that the oligosaccharides isolated form a cwh41 delta null mutant are fully glucosylated, retaining the three terminal glucose residues, whereas the oligosaccharides from CWH41 cells do not have any glucose residues. These results showing a lack of glucosidase I activity in cwh41 delta null mutants both in vitro and in vivo are consistent with the structural evidence that CWH41 encodes the yeast glucosidase I."}