Loading…
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...
Saved in:
Published in: | Biochemical and biophysical research communications 1997-03, Vol.232 (1), p.121-125 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | |
container_end_page | 125 |
container_issue | 1 |
container_start_page | 121 |
container_title | Biochemical and biophysical research communications |
container_volume | 232 |
creator | Tabuchi, M Tanaka, N Iwahara, S Takegawa, K |
description | 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. |
doi_str_mv | 10.1006/bbrc.1997.6239 |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_78907710</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>78907710</sourcerecordid><originalsourceid>FETCH-LOGICAL-p206t-66816360329a61c139622d969088ee126e335df3637c589e3805cd7f3fa99cbe3</originalsourceid><addsrcrecordid>eNo1ULtOwzAU9QAqpbCyIXliQSl-ECceUSkPqRJItBJb5Dg3DxTbqe0MRXw8kSjTObrnoauD0BUlS0qIuCtLr5dUymwpGJcnaE6ma8Ik_TxD5yF8EULpvZAzNJOUpROfo59tC_hDt923C0rrVnlnDhoCHpwpATcm0FvcgAUMVrtqEpTFu8f3pFG90tEFwNErGwbnI3jcOuN614yAPezHzkOFa-fx4F2EzuL_0KFXsXP2Ap3Wqg9wecQF2j2tt6uXZPP2_Lp62CQDIyImQuRUcEE4k0pQTbkUjFVSSJLnAJQJ4Dytai54ptNcAs9Jqqus5rWSUpfAF-jmr3f6Yz9CiIXpgoa-VxbcGIoslyTLKJmM10fjWBqoisF3RvlDcZyL_wKO_2yN</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>78907710</pqid></control><display><type>article</type><title>The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation</title><source>ScienceDirect Freedom Collection</source><creator>Tabuchi, M ; Tanaka, N ; Iwahara, S ; Takegawa, K</creator><creatorcontrib>Tabuchi, M ; Tanaka, N ; Iwahara, S ; Takegawa, K</creatorcontrib><description>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.</description><identifier>ISSN: 0006-291X</identifier><identifier>DOI: 10.1006/bbrc.1997.6239</identifier><identifier>PMID: 9125114</identifier><language>eng</language><publisher>United States</publisher><subject>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</subject><ispartof>Biochemical and biophysical research communications, 1997-03, Vol.232 (1), p.121-125</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9125114$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tabuchi, M</creatorcontrib><creatorcontrib>Tanaka, N</creatorcontrib><creatorcontrib>Iwahara, S</creatorcontrib><creatorcontrib>Takegawa, K</creatorcontrib><title>The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Biological Transport</subject><subject>DNA, Recombinant</subject><subject>Genes, Fungal</subject><subject>Golgi Apparatus - metabolism</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Monosaccharide Transport Proteins - genetics</subject><subject>Monosaccharide Transport Proteins - metabolism</subject><subject>Schizosaccharomyces - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Uridine Diphosphate Galactose - metabolism</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNo1ULtOwzAU9QAqpbCyIXliQSl-ECceUSkPqRJItBJb5Dg3DxTbqe0MRXw8kSjTObrnoauD0BUlS0qIuCtLr5dUymwpGJcnaE6ma8Ik_TxD5yF8EULpvZAzNJOUpROfo59tC_hDt923C0rrVnlnDhoCHpwpATcm0FvcgAUMVrtqEpTFu8f3pFG90tEFwNErGwbnI3jcOuN614yAPezHzkOFa-fx4F2EzuL_0KFXsXP2Ap3Wqg9wecQF2j2tt6uXZPP2_Lp62CQDIyImQuRUcEE4k0pQTbkUjFVSSJLnAJQJ4Dytai54ptNcAs9Jqqus5rWSUpfAF-jmr3f6Yz9CiIXpgoa-VxbcGIoslyTLKJmM10fjWBqoisF3RvlDcZyL_wKO_2yN</recordid><startdate>19970306</startdate><enddate>19970306</enddate><creator>Tabuchi, M</creator><creator>Tanaka, N</creator><creator>Iwahara, S</creator><creator>Takegawa, K</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19970306</creationdate><title>The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation</title><author>Tabuchi, M ; Tanaka, N ; Iwahara, S ; Takegawa, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p206t-66816360329a61c139622d969088ee126e335df3637c589e3805cd7f3fa99cbe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Biological Transport</topic><topic>DNA, Recombinant</topic><topic>Genes, Fungal</topic><topic>Golgi Apparatus - metabolism</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Monosaccharide Transport Proteins - genetics</topic><topic>Monosaccharide Transport Proteins - metabolism</topic><topic>Schizosaccharomyces - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Uridine Diphosphate Galactose - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tabuchi, M</creatorcontrib><creatorcontrib>Tanaka, N</creatorcontrib><creatorcontrib>Iwahara, S</creatorcontrib><creatorcontrib>Takegawa, K</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tabuchi, M</au><au>Tanaka, N</au><au>Iwahara, S</au><au>Takegawa, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1997-03-06</date><risdate>1997</risdate><volume>232</volume><issue>1</issue><spage>121</spage><epage>125</epage><pages>121-125</pages><issn>0006-291X</issn><abstract>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.</abstract><cop>United States</cop><pmid>9125114</pmid><doi>10.1006/bbrc.1997.6239</doi><tpages>5</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-291X |
ispartof | Biochemical and biophysical research communications, 1997-03, Vol.232 (1), p.121-125 |
issn | 0006-291X |
language | eng |
recordid | cdi_proquest_miscellaneous_78907710 |
source | ScienceDirect Freedom Collection |
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 |
title | The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T15%3A04%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Schizosaccharomyces%20pombe%20gms1+%20gene%20encodes%20an%20UDP-galactose%20transporter%20homologue%20required%20for%20protein%20galactosylation&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Tabuchi,%20M&rft.date=1997-03-06&rft.volume=232&rft.issue=1&rft.spage=121&rft.epage=125&rft.pages=121-125&rft.issn=0006-291X&rft_id=info:doi/10.1006/bbrc.1997.6239&rft_dat=%3Cproquest_pubme%3E78907710%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p206t-66816360329a61c139622d969088ee126e335df3637c589e3805cd7f3fa99cbe3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=78907710&rft_id=info:pmid/9125114&rfr_iscdi=true |