Cloning, expression, and characterization of cytosolic sulfotransferase isozymes from Drosophila melanogaster
We have identified four cytosolic sulfotransferase (SULT) homologs in the genome database of Drosophila melanogaster, and have designated these genes dmST1-4. Each of these four isozymes was subsequently classified into a different and novel gene family, as determined by the low amino acid sequence...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2008-02, Vol.72 (2), p.540-547 |
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| creator | Hattori, K.(Kyoritsu Univ. of Pharmacy, Tokyo (Japan)) Motohashi, N Kobayashi, I Tohya, T Oikawa, M Tamura, H |
| description | We have identified four cytosolic sulfotransferase (SULT) homologs in the genome database of Drosophila melanogaster, and have designated these genes dmST1-4. Each of these four isozymes was subsequently classified into a different and novel gene family, as determined by the low amino acid sequence homology (less than 40%) between them, and also toward their vertebrate homologs. The transcripts for these four SULT homologs were detectable at all developmental stages in D. melanogaster. In addition, three of these isozymes, the exception being dmST2, were successfully expressed and purified in Escherichia coli. These recombinant dmST1, 3, and 4 products showed high sulfating activity toward phenolic compounds such as vanillin and 4-nitrophenol, but showed no activity toward typical endogenous substrates such as tyramine and serotonin. DmST4 and dmST3 showed the lowest and highest Ksub(m) values for 3'-phosphoadenosine-5'-phosphosulfate (PAPS) respectively. DmST4 also showed low but not negligible activity toward 20-hydroxyecdysone. |
| doi_str_mv | 10.1271/bbb.70647 |
| format | Article |
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Each of these four isozymes was subsequently classified into a different and novel gene family, as determined by the low amino acid sequence homology (less than 40%) between them, and also toward their vertebrate homologs. The transcripts for these four SULT homologs were detectable at all developmental stages in D. melanogaster. In addition, three of these isozymes, the exception being dmST2, were successfully expressed and purified in Escherichia coli. These recombinant dmST1, 3, and 4 products showed high sulfating activity toward phenolic compounds such as vanillin and 4-nitrophenol, but showed no activity toward typical endogenous substrates such as tyramine and serotonin. DmST4 and dmST3 showed the lowest and highest Ksub(m) values for 3'-phosphoadenosine-5'-phosphosulfate (PAPS) respectively. DmST4 also showed low but not negligible activity toward 20-hydroxyecdysone.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.70647</identifier><identifier>PMID: 18256476</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Amino Acid Sequence ; AMINO ACID SEQUENCES ; Animals ; aryl sulfotransferase ; Base Sequence ; Biological and medical sciences ; CHOLESTEROL ; CLONACION ; CLONAGE ; CLONING ; Cloning, Molecular ; COLESTEROL ; COMPOSE PHENOLIQUE ; COMPUESTOS FENOLICOS ; Cytosol - enzymology ; DNA Primers ; DROSOPHILA MELANOGASTER ; Escherichia coli ; EXPRESION GENICA ; EXPRESSION DES GENES ; Fundamental and applied biological sciences. Psychology ; GENE EXPRESSION ; Gene Expression Profiling ; insect ; INSECTA ; Molecular Sequence Data ; PHENOLIC COMPOUNDS ; Phylogeny ; PROTEINAS RECOMBINANTES ; PROTEINE RECOMBINANTE ; RECOMBINANT PROTEINS ; Reverse Transcriptase Polymerase Chain Reaction ; SECUENCIAS DE AMINOACIDOS ; SEQUENCE D'ACIDES AMINES ; Sequence Homology, Amino Acid ; Sulfotransferases - chemistry ; Sulfotransferases - genetics ; Sulfotransferases - metabolism</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2008-02, Vol.72 (2), p.540-547</ispartof><rights>2008 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2008</rights><rights>2008 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2008</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c565t-fa7b8993766f0055de626a26e99a34df24a77673a1a19379340582a8962e87763</citedby><cites>FETCH-LOGICAL-c565t-fa7b8993766f0055de626a26e99a34df24a77673a1a19379340582a8962e87763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20232933$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18256476$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hattori, K.(Kyoritsu Univ. of Pharmacy, Tokyo (Japan))</creatorcontrib><creatorcontrib>Motohashi, N</creatorcontrib><creatorcontrib>Kobayashi, I</creatorcontrib><creatorcontrib>Tohya, T</creatorcontrib><creatorcontrib>Oikawa, M</creatorcontrib><creatorcontrib>Tamura, H</creatorcontrib><title>Cloning, expression, and characterization of cytosolic sulfotransferase isozymes from Drosophila melanogaster</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>We have identified four cytosolic sulfotransferase (SULT) homologs in the genome database of Drosophila melanogaster, and have designated these genes dmST1-4. Each of these four isozymes was subsequently classified into a different and novel gene family, as determined by the low amino acid sequence homology (less than 40%) between them, and also toward their vertebrate homologs. The transcripts for these four SULT homologs were detectable at all developmental stages in D. melanogaster. In addition, three of these isozymes, the exception being dmST2, were successfully expressed and purified in Escherichia coli. These recombinant dmST1, 3, and 4 products showed high sulfating activity toward phenolic compounds such as vanillin and 4-nitrophenol, but showed no activity toward typical endogenous substrates such as tyramine and serotonin. DmST4 and dmST3 showed the lowest and highest Ksub(m) values for 3'-phosphoadenosine-5'-phosphosulfate (PAPS) respectively. DmST4 also showed low but not negligible activity toward 20-hydroxyecdysone.</description><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Animals</subject><subject>aryl sulfotransferase</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>CHOLESTEROL</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>CLONING</subject><subject>Cloning, Molecular</subject><subject>COLESTEROL</subject><subject>COMPOSE PHENOLIQUE</subject><subject>COMPUESTOS FENOLICOS</subject><subject>Cytosol - enzymology</subject><subject>DNA Primers</subject><subject>DROSOPHILA MELANOGASTER</subject><subject>Escherichia coli</subject><subject>EXPRESION GENICA</subject><subject>EXPRESSION DES GENES</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENE EXPRESSION</subject><subject>Gene Expression Profiling</subject><subject>insect</subject><subject>INSECTA</subject><subject>Molecular Sequence Data</subject><subject>PHENOLIC COMPOUNDS</subject><subject>Phylogeny</subject><subject>PROTEINAS RECOMBINANTES</subject><subject>PROTEINE RECOMBINANTE</subject><subject>RECOMBINANT PROTEINS</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>SECUENCIAS DE AMINOACIDOS</subject><subject>SEQUENCE D'ACIDES AMINES</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sulfotransferases - chemistry</subject><subject>Sulfotransferases - genetics</subject><subject>Sulfotransferases - metabolism</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0cuKFDEUBuAgitOOLnwAJSAKwtSY-2Up7Z0BXeg6nKpOejKkKj1JFdrz9Ea7VRDBVSD5zklOfoQeUnJOmaYv-r4_10QJfQutKBe6U1bo22hFLFWdEZKeoHu1XhHSNiS9i06oYbJxtULjOuUpTtsz7L_tiq815ukMw7TBwyUUGGZf4g3MbRfngIf9nGtOccB1SSHPBaYafIHqcaz5Zj_6ikPJI35VmttdxgR49AmmvIXaWt1HdwKk6h8c11P05c3rz-t33cXHt-_XLy-6QSo5dwF0b6zlWqlAiJQbr5gCpry1wMUmMAFaK82BAm3KckGkYWCsYt60E36Knh367kq-Xnyd3Rjr4FN7ic9LdZpwZq2k_4XUGm2pJQ0--Qte5aVMbQhHhbCGMaZMU88Pamjz1-KD25U4Qtk7StyPqFyLyv2MqtnHx45LP_rNH3nMpoGnRwB1gBTaZw-x_naMsDYE582Jg4tTyGWEr7mkjZthn3L5VcT_df-jQ1mA7GBbmvrwiRFiCBHaSP4dB4y2ew</recordid><startdate>20080201</startdate><enddate>20080201</enddate><creator>Hattori, K.(Kyoritsu Univ. of Pharmacy, Tokyo (Japan))</creator><creator>Motohashi, N</creator><creator>Kobayashi, I</creator><creator>Tohya, T</creator><creator>Oikawa, M</creator><creator>Tamura, H</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</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>7QL</scope><scope>7SS</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20080201</creationdate><title>Cloning, expression, and characterization of cytosolic sulfotransferase isozymes from Drosophila melanogaster</title><author>Hattori, K.(Kyoritsu Univ. of Pharmacy, Tokyo (Japan)) ; Motohashi, N ; Kobayashi, I ; Tohya, T ; Oikawa, M ; Tamura, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c565t-fa7b8993766f0055de626a26e99a34df24a77673a1a19379340582a8962e87763</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Animals</topic><topic>aryl sulfotransferase</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>CHOLESTEROL</topic><topic>CLONACION</topic><topic>CLONAGE</topic><topic>CLONING</topic><topic>Cloning, Molecular</topic><topic>COLESTEROL</topic><topic>COMPOSE PHENOLIQUE</topic><topic>COMPUESTOS FENOLICOS</topic><topic>Cytosol - enzymology</topic><topic>DNA Primers</topic><topic>DROSOPHILA MELANOGASTER</topic><topic>Escherichia coli</topic><topic>EXPRESION GENICA</topic><topic>EXPRESSION DES GENES</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENE EXPRESSION</topic><topic>Gene Expression Profiling</topic><topic>insect</topic><topic>INSECTA</topic><topic>Molecular Sequence Data</topic><topic>PHENOLIC COMPOUNDS</topic><topic>Phylogeny</topic><topic>PROTEINAS RECOMBINANTES</topic><topic>PROTEINE RECOMBINANTE</topic><topic>RECOMBINANT PROTEINS</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>SECUENCIAS DE AMINOACIDOS</topic><topic>SEQUENCE D'ACIDES AMINES</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sulfotransferases - chemistry</topic><topic>Sulfotransferases - genetics</topic><topic>Sulfotransferases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hattori, K.(Kyoritsu Univ. of Pharmacy, Tokyo (Japan))</creatorcontrib><creatorcontrib>Motohashi, N</creatorcontrib><creatorcontrib>Kobayashi, I</creatorcontrib><creatorcontrib>Tohya, T</creatorcontrib><creatorcontrib>Oikawa, M</creatorcontrib><creatorcontrib>Tamura, H</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hattori, K.(Kyoritsu Univ. of Pharmacy, Tokyo (Japan))</au><au>Motohashi, N</au><au>Kobayashi, I</au><au>Tohya, T</au><au>Oikawa, M</au><au>Tamura, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, expression, and characterization of cytosolic sulfotransferase isozymes from Drosophila melanogaster</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2008-02-01</date><risdate>2008</risdate><volume>72</volume><issue>2</issue><spage>540</spage><epage>547</epage><pages>540-547</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>We have identified four cytosolic sulfotransferase (SULT) homologs in the genome database of Drosophila melanogaster, and have designated these genes dmST1-4. Each of these four isozymes was subsequently classified into a different and novel gene family, as determined by the low amino acid sequence homology (less than 40%) between them, and also toward their vertebrate homologs. The transcripts for these four SULT homologs were detectable at all developmental stages in D. melanogaster. In addition, three of these isozymes, the exception being dmST2, were successfully expressed and purified in Escherichia coli. These recombinant dmST1, 3, and 4 products showed high sulfating activity toward phenolic compounds such as vanillin and 4-nitrophenol, but showed no activity toward typical endogenous substrates such as tyramine and serotonin. DmST4 and dmST3 showed the lowest and highest Ksub(m) values for 3'-phosphoadenosine-5'-phosphosulfate (PAPS) respectively. DmST4 also showed low but not negligible activity toward 20-hydroxyecdysone.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>18256476</pmid><doi>10.1271/bbb.70647</doi><tpages>8</tpages></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 2008-02, Vol.72 (2), p.540-547 |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence AMINO ACID SEQUENCES Animals aryl sulfotransferase Base Sequence Biological and medical sciences CHOLESTEROL CLONACION CLONAGE CLONING Cloning, Molecular COLESTEROL COMPOSE PHENOLIQUE COMPUESTOS FENOLICOS Cytosol - enzymology DNA Primers DROSOPHILA MELANOGASTER Escherichia coli EXPRESION GENICA EXPRESSION DES GENES Fundamental and applied biological sciences. Psychology GENE EXPRESSION Gene Expression Profiling insect INSECTA Molecular Sequence Data PHENOLIC COMPOUNDS Phylogeny PROTEINAS RECOMBINANTES PROTEINE RECOMBINANTE RECOMBINANT PROTEINS Reverse Transcriptase Polymerase Chain Reaction SECUENCIAS DE AMINOACIDOS SEQUENCE D'ACIDES AMINES Sequence Homology, Amino Acid Sulfotransferases - chemistry Sulfotransferases - genetics Sulfotransferases - metabolism |
| title | Cloning, expression, and characterization of cytosolic sulfotransferase isozymes from Drosophila melanogaster |
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