Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase
UDP-glucose:glycoprotein glucose-1-phosphotransferase (Glc-phosphotransferase) catalyzes the transfer of Glc-1-P from UDP-Glc to mannose residues on acceptor glycoproteins. The predominant acceptor in vertebrates and Paramecium tetraurelia is a cytoplasmic 62-kDa glycoprotein. To determine if the ye...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-04, Vol.268 (11), p.8341-8349 |
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| container_title | The Journal of biological chemistry |
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| creator | Marchase, R.B Bounelis, P Brumley, L.M Dey, N Browne, B Auger, D Fritz, T.A Kulesza, P Bedwell, D.M |
| description | UDP-glucose:glycoprotein glucose-1-phosphotransferase (Glc-phosphotransferase) catalyzes the transfer of Glc-1-P from UDP-Glc to mannose residues on acceptor glycoproteins. The predominant acceptor in vertebrates and Paramecium tetraurelia is a cytoplasmic 62-kDa glycoprotein. To determine if the yeast Saccharomyces cerevisiae also possesses Glc-phosphotransferase activity, a crude cellular lysate was incubated with [beta-32P]UDP-Glc and analyzed. A phosphoglycoprotein having an apparent molecular mass of 62 kDa (pgp62) was found to be the predominant labeled macromolecule. Reconstitution experiments determined that both a soluble and membrane fraction were required for labeling, and suggested that the Glc-phosphotransferase is membrane-associated while pgp62 is cytoplasmic. The reaction is evolutionarily conserved to the extent that rat liver Glc-phosphotransferase was capable of recognizing the yeast acceptor and vice versa. The yeast 62-kDa acceptor was purified, and partial amino acid sequences showed a high level of identity with rabbit muscle phosphoglucomutase. Subsequently, both yeast and rabbit muscle phosphoglucomutase were found to be acceptors in the Glc-phosphotransferase reaction. The label was found on a tryptic peptide distinct from that containing the enzyme's active site serine. When phosphoglucomutase was overexpressed, an increase was seen in Glc-phosphotransferase acceptor activity and in specific metabolic labeling of the acceptor by glucose and mannose |
| doi_str_mv | 10.1016/S0021-9258(18)53101-X |
| format | Article |
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The predominant acceptor in vertebrates and Paramecium tetraurelia is a cytoplasmic 62-kDa glycoprotein. To determine if the yeast Saccharomyces cerevisiae also possesses Glc-phosphotransferase activity, a crude cellular lysate was incubated with [beta-32P]UDP-Glc and analyzed. A phosphoglycoprotein having an apparent molecular mass of 62 kDa (pgp62) was found to be the predominant labeled macromolecule. Reconstitution experiments determined that both a soluble and membrane fraction were required for labeling, and suggested that the Glc-phosphotransferase is membrane-associated while pgp62 is cytoplasmic. The reaction is evolutionarily conserved to the extent that rat liver Glc-phosphotransferase was capable of recognizing the yeast acceptor and vice versa. The yeast 62-kDa acceptor was purified, and partial amino acid sequences showed a high level of identity with rabbit muscle phosphoglucomutase. Subsequently, both yeast and rabbit muscle phosphoglucomutase were found to be acceptors in the Glc-phosphotransferase reaction. The label was found on a tryptic peptide distinct from that containing the enzyme's active site serine. When phosphoglucomutase was overexpressed, an increase was seen in Glc-phosphotransferase acceptor activity and in specific metabolic labeling of the acceptor by glucose and mannose</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)53101-X</identifier><identifier>PMID: 8385141</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; CITOPLASMA ; Cytoplasm - enzymology ; CYTOPLASME ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Genes, Fungal ; GLICOPROTEINAS ; Glucose - metabolism ; GLYCOPROTEINE ; Glycoproteins - metabolism ; ISOMERASAS ; ISOMERASE ; Mannose - metabolism ; Methionine - metabolism ; Miscellaneous ; Molecular Sequence Data ; Muscles - enzymology ; Mutation ; Phosphoglucomutase - genetics ; Phosphoglucomutase - isolation & purification ; Phosphoglucomutase - metabolism ; Phosphorus Radioisotopes ; Phosphotransferases - metabolism ; Plasmids ; Rabbits ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Sequence Homology, Amino Acid ; Substrate Specificity ; TRANSFERASAS ; TRANSFERASE ; Transferases (Other Substituted Phosphate Groups) ; Uridine Diphosphate Glucose - metabolism</subject><ispartof>The Journal of biological chemistry, 1993-04, Vol.268 (11), p.8341-8349</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-574b072649fdcc0f248d4158f62affdc985eca7d9afeeb397b946057167c97a73</citedby><cites>FETCH-LOGICAL-c427t-574b072649fdcc0f248d4158f62affdc985eca7d9afeeb397b946057167c97a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4747506$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8385141$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marchase, R.B</creatorcontrib><creatorcontrib>Bounelis, P</creatorcontrib><creatorcontrib>Brumley, L.M</creatorcontrib><creatorcontrib>Dey, N</creatorcontrib><creatorcontrib>Browne, B</creatorcontrib><creatorcontrib>Auger, D</creatorcontrib><creatorcontrib>Fritz, T.A</creatorcontrib><creatorcontrib>Kulesza, P</creatorcontrib><creatorcontrib>Bedwell, D.M</creatorcontrib><title>Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>UDP-glucose:glycoprotein glucose-1-phosphotransferase (Glc-phosphotransferase) catalyzes the transfer of Glc-1-P from UDP-Glc to mannose residues on acceptor glycoproteins. The predominant acceptor in vertebrates and Paramecium tetraurelia is a cytoplasmic 62-kDa glycoprotein. To determine if the yeast Saccharomyces cerevisiae also possesses Glc-phosphotransferase activity, a crude cellular lysate was incubated with [beta-32P]UDP-Glc and analyzed. A phosphoglycoprotein having an apparent molecular mass of 62 kDa (pgp62) was found to be the predominant labeled macromolecule. Reconstitution experiments determined that both a soluble and membrane fraction were required for labeling, and suggested that the Glc-phosphotransferase is membrane-associated while pgp62 is cytoplasmic. The reaction is evolutionarily conserved to the extent that rat liver Glc-phosphotransferase was capable of recognizing the yeast acceptor and vice versa. The yeast 62-kDa acceptor was purified, and partial amino acid sequences showed a high level of identity with rabbit muscle phosphoglucomutase. Subsequently, both yeast and rabbit muscle phosphoglucomutase were found to be acceptors in the Glc-phosphotransferase reaction. The label was found on a tryptic peptide distinct from that containing the enzyme's active site serine. When phosphoglucomutase was overexpressed, an increase was seen in Glc-phosphotransferase acceptor activity and in specific metabolic labeling of the acceptor by glucose and mannose</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>CITOPLASMA</subject><subject>Cytoplasm - enzymology</subject><subject>CYTOPLASME</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Fungal</subject><subject>GLICOPROTEINAS</subject><subject>Glucose - metabolism</subject><subject>GLYCOPROTEINE</subject><subject>Glycoproteins - metabolism</subject><subject>ISOMERASAS</subject><subject>ISOMERASE</subject><subject>Mannose - metabolism</subject><subject>Methionine - metabolism</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Muscles - enzymology</subject><subject>Mutation</subject><subject>Phosphoglucomutase - genetics</subject><subject>Phosphoglucomutase - isolation & purification</subject><subject>Phosphoglucomutase - metabolism</subject><subject>Phosphorus Radioisotopes</subject><subject>Phosphotransferases - metabolism</subject><subject>Plasmids</subject><subject>Rabbits</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate Specificity</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>Transferases (Other Substituted Phosphate Groups)</subject><subject>Uridine Diphosphate Glucose - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kFFr2zAUhcXY6NJuf2BQEGyM7cGbZEmW9VjK2g0KLWSFvIlrWYo17MiT7I3011eNQwRCcO93zhEHoUtKvlFCq-9rQkpaqFLUX2j9VbA8LDav0IqSmhVM0M1rtDohb9F5Sn9IPlzRM3RWs1pQTlfo6aELaezCtp9NGOYJksV-h9dgTAcxDHtjEzY22n8-eci7hAGb_RTGHtLgDd72exPGGCabZbBr8dRZnNV2nELELl_At70pxiVnirBLzsac8w69cdAn-_74XqDHmx-_r38Wd_e3v66v7grDSzkVQvKGyLLiyrXGEFfyuuVU1K4qweWRqoU1IFsFztqGKdkoXhEhaSWNkiDZBfq8-OZf_p1tmvTgk7F9Dzsb5qSlqASlrMygWEATQ0rROj1GP0Dca0r0S-f60Ll-KVTTWh8615usuzwGzM1g25PqWHLefzruIRnoXa7A-HTCuORSkCpjHxes89vuv49WNz6Yzg66rHIezX4Hsw8L5SBo2MZs9LhWnBEmFHsGP9qgew</recordid><startdate>19930415</startdate><enddate>19930415</enddate><creator>Marchase, R.B</creator><creator>Bounelis, P</creator><creator>Brumley, L.M</creator><creator>Dey, N</creator><creator>Browne, B</creator><creator>Auger, D</creator><creator>Fritz, T.A</creator><creator>Kulesza, P</creator><creator>Bedwell, D.M</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19930415</creationdate><title>Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase</title><author>Marchase, R.B ; Bounelis, P ; Brumley, L.M ; Dey, N ; Browne, B ; Auger, D ; Fritz, T.A ; Kulesza, P ; Bedwell, D.M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-574b072649fdcc0f248d4158f62affdc985eca7d9afeeb397b946057167c97a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>CITOPLASMA</topic><topic>Cytoplasm - enzymology</topic><topic>CYTOPLASME</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genes, Fungal</topic><topic>GLICOPROTEINAS</topic><topic>Glucose - metabolism</topic><topic>GLYCOPROTEINE</topic><topic>Glycoproteins - metabolism</topic><topic>ISOMERASAS</topic><topic>ISOMERASE</topic><topic>Mannose - metabolism</topic><topic>Methionine - metabolism</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Muscles - enzymology</topic><topic>Mutation</topic><topic>Phosphoglucomutase - genetics</topic><topic>Phosphoglucomutase - isolation & purification</topic><topic>Phosphoglucomutase - metabolism</topic><topic>Phosphorus Radioisotopes</topic><topic>Phosphotransferases - metabolism</topic><topic>Plasmids</topic><topic>Rabbits</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate Specificity</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>Transferases (Other Substituted Phosphate Groups)</topic><topic>Uridine Diphosphate Glucose - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marchase, R.B</creatorcontrib><creatorcontrib>Bounelis, P</creatorcontrib><creatorcontrib>Brumley, L.M</creatorcontrib><creatorcontrib>Dey, N</creatorcontrib><creatorcontrib>Browne, B</creatorcontrib><creatorcontrib>Auger, D</creatorcontrib><creatorcontrib>Fritz, T.A</creatorcontrib><creatorcontrib>Kulesza, P</creatorcontrib><creatorcontrib>Bedwell, D.M</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marchase, R.B</au><au>Bounelis, P</au><au>Brumley, L.M</au><au>Dey, N</au><au>Browne, B</au><au>Auger, D</au><au>Fritz, T.A</au><au>Kulesza, P</au><au>Bedwell, D.M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-04-15</date><risdate>1993</risdate><volume>268</volume><issue>11</issue><spage>8341</spage><epage>8349</epage><pages>8341-8349</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>UDP-glucose:glycoprotein glucose-1-phosphotransferase (Glc-phosphotransferase) catalyzes the transfer of Glc-1-P from UDP-Glc to mannose residues on acceptor glycoproteins. The predominant acceptor in vertebrates and Paramecium tetraurelia is a cytoplasmic 62-kDa glycoprotein. To determine if the yeast Saccharomyces cerevisiae also possesses Glc-phosphotransferase activity, a crude cellular lysate was incubated with [beta-32P]UDP-Glc and analyzed. A phosphoglycoprotein having an apparent molecular mass of 62 kDa (pgp62) was found to be the predominant labeled macromolecule. Reconstitution experiments determined that both a soluble and membrane fraction were required for labeling, and suggested that the Glc-phosphotransferase is membrane-associated while pgp62 is cytoplasmic. The reaction is evolutionarily conserved to the extent that rat liver Glc-phosphotransferase was capable of recognizing the yeast acceptor and vice versa. The yeast 62-kDa acceptor was purified, and partial amino acid sequences showed a high level of identity with rabbit muscle phosphoglucomutase. Subsequently, both yeast and rabbit muscle phosphoglucomutase were found to be acceptors in the Glc-phosphotransferase reaction. The label was found on a tryptic peptide distinct from that containing the enzyme's active site serine. When phosphoglucomutase was overexpressed, an increase was seen in Glc-phosphotransferase acceptor activity and in specific metabolic labeling of the acceptor by glucose and mannose</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8385141</pmid><doi>10.1016/S0021-9258(18)53101-X</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-04, Vol.268 (11), p.8341-8349 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences CITOPLASMA Cytoplasm - enzymology CYTOPLASME Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Genes, Fungal GLICOPROTEINAS Glucose - metabolism GLYCOPROTEINE Glycoproteins - metabolism ISOMERASAS ISOMERASE Mannose - metabolism Methionine - metabolism Miscellaneous Molecular Sequence Data Muscles - enzymology Mutation Phosphoglucomutase - genetics Phosphoglucomutase - isolation & purification Phosphoglucomutase - metabolism Phosphorus Radioisotopes Phosphotransferases - metabolism Plasmids Rabbits SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Sequence Homology, Amino Acid Substrate Specificity TRANSFERASAS TRANSFERASE Transferases (Other Substituted Phosphate Groups) Uridine Diphosphate Glucose - metabolism |
| title | Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase |
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