Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura
Two cDNAs encoding glutathione S‐transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase‐polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon‐class GSTs from other organisms. The recomb...
Gespeichert in:
| Veröffentlicht in: | Archives of insect biochemistry and physiology 2018-03, Vol.97 (3), p.n/a |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | n/a |
|---|---|
| container_issue | 3 |
| container_start_page | |
| container_title | Archives of insect biochemistry and physiology |
| container_volume | 97 |
| creator | Hirowatari, Aiko Chen, Zhiwei Mita, Kazuei Yamamoto, Kohji |
| description | Two cDNAs encoding glutathione S‐transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase‐polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon‐class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1‐chloro‐2,4‐dinitrobenzene, 1,2‐epoxy‐3‐(4‐nitrophenoxy)‐propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm. |
| doi_str_mv | 10.1002/arch.21443 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1976443485</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1976443485</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3573-cd12f0d7b1f87a5c1b22e1e1b51e1701d2c8603f8fcee59b49f6fd9688023ee63</originalsourceid><addsrcrecordid>eNp9kE1LwzAYgIMobk4v_gApeBGhMx9N2h5l-AUDwY9zSNM3rqNratIy5smf4G_0l5i56cGDl4SE5314eRA6JnhMMKYXyunZmJIkYTtoSDjFsWA03UVDnLI8ThJBB-jA-znGOBck20cDmlPGRc6HSF81b6uF6iod6ZlySnfgqrfwtk1kTdQtbQStr2rbfL5_6Fp5H73Ufae6WSAgegy_nVONN-CUB7-eeWxtadvgUVFddb1Th2jPqNrD0fYeoefrq6fJbTy9v7mbXE5jzXjKYl0SanCZFsRkqeKaFJQCAVLwcKSYlFRnAjOTGQ3A8yLJjTBlLrIMUwYg2Aidbbyts689-E4uKq-hrlUDtveS5KkIkZKMB_T0Dzq3vWvCdpJiTGjCOU8Cdb6htLPeOzCyddVCuZUkWK7Ty3V6-Z0-wCdbZV8soPxFf1oHgGyAZVXD6h-VvHyY3G6kX-7mkZI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2001245554</pqid></control><display><type>article</type><title>Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura</title><source>Wiley Online Library Journals Frontfile Complete</source><creator>Hirowatari, Aiko ; Chen, Zhiwei ; Mita, Kazuei ; Yamamoto, Kohji</creator><creatorcontrib>Hirowatari, Aiko ; Chen, Zhiwei ; Mita, Kazuei ; Yamamoto, Kohji</creatorcontrib><description>Two cDNAs encoding glutathione S‐transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase‐polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon‐class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1‐chloro‐2,4‐dinitrobenzene, 1,2‐epoxy‐3‐(4‐nitrophenoxy)‐propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.</description><identifier>ISSN: 0739-4462</identifier><identifier>EISSN: 1520-6327</identifier><identifier>DOI: 10.1002/arch.21443</identifier><identifier>PMID: 29235695</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>1-Chloro-2,4-dinitrobenzene ; Dinitrobenzene ; E coli ; Ethacrynic acid ; Glutathione ; Glutathione transferase ; Homogeneity ; Insecticides ; Lepidoptera ; Polymerase chain reaction ; Proteins ; RNA-directed DNA polymerase ; Spodoptera litura ; Tobacco</subject><ispartof>Archives of insect biochemistry and physiology, 2018-03, Vol.97 (3), p.n/a</ispartof><rights>2017 Wiley Periodicals, Inc.</rights><rights>Copyright © 2018 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3573-cd12f0d7b1f87a5c1b22e1e1b51e1701d2c8603f8fcee59b49f6fd9688023ee63</citedby><cites>FETCH-LOGICAL-c3573-cd12f0d7b1f87a5c1b22e1e1b51e1701d2c8603f8fcee59b49f6fd9688023ee63</cites><orcidid>0000-0002-5859-912X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Farch.21443$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Farch.21443$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29235695$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hirowatari, Aiko</creatorcontrib><creatorcontrib>Chen, Zhiwei</creatorcontrib><creatorcontrib>Mita, Kazuei</creatorcontrib><creatorcontrib>Yamamoto, Kohji</creatorcontrib><title>Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura</title><title>Archives of insect biochemistry and physiology</title><addtitle>Arch Insect Biochem Physiol</addtitle><description>Two cDNAs encoding glutathione S‐transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase‐polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon‐class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1‐chloro‐2,4‐dinitrobenzene, 1,2‐epoxy‐3‐(4‐nitrophenoxy)‐propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.</description><subject>1-Chloro-2,4-dinitrobenzene</subject><subject>Dinitrobenzene</subject><subject>E coli</subject><subject>Ethacrynic acid</subject><subject>Glutathione</subject><subject>Glutathione transferase</subject><subject>Homogeneity</subject><subject>Insecticides</subject><subject>Lepidoptera</subject><subject>Polymerase chain reaction</subject><subject>Proteins</subject><subject>RNA-directed DNA polymerase</subject><subject>Spodoptera litura</subject><subject>Tobacco</subject><issn>0739-4462</issn><issn>1520-6327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp9kE1LwzAYgIMobk4v_gApeBGhMx9N2h5l-AUDwY9zSNM3rqNratIy5smf4G_0l5i56cGDl4SE5314eRA6JnhMMKYXyunZmJIkYTtoSDjFsWA03UVDnLI8ThJBB-jA-znGOBck20cDmlPGRc6HSF81b6uF6iod6ZlySnfgqrfwtk1kTdQtbQStr2rbfL5_6Fp5H73Ufae6WSAgegy_nVONN-CUB7-eeWxtadvgUVFddb1Th2jPqNrD0fYeoefrq6fJbTy9v7mbXE5jzXjKYl0SanCZFsRkqeKaFJQCAVLwcKSYlFRnAjOTGQ3A8yLJjTBlLrIMUwYg2Aidbbyts689-E4uKq-hrlUDtveS5KkIkZKMB_T0Dzq3vWvCdpJiTGjCOU8Cdb6htLPeOzCyddVCuZUkWK7Ty3V6-Z0-wCdbZV8soPxFf1oHgGyAZVXD6h-VvHyY3G6kX-7mkZI</recordid><startdate>201803</startdate><enddate>201803</enddate><creator>Hirowatari, Aiko</creator><creator>Chen, Zhiwei</creator><creator>Mita, Kazuei</creator><creator>Yamamoto, Kohji</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QR</scope><scope>7SS</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-5859-912X</orcidid></search><sort><creationdate>201803</creationdate><title>Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura</title><author>Hirowatari, Aiko ; Chen, Zhiwei ; Mita, Kazuei ; Yamamoto, Kohji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3573-cd12f0d7b1f87a5c1b22e1e1b51e1701d2c8603f8fcee59b49f6fd9688023ee63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>1-Chloro-2,4-dinitrobenzene</topic><topic>Dinitrobenzene</topic><topic>E coli</topic><topic>Ethacrynic acid</topic><topic>Glutathione</topic><topic>Glutathione transferase</topic><topic>Homogeneity</topic><topic>Insecticides</topic><topic>Lepidoptera</topic><topic>Polymerase chain reaction</topic><topic>Proteins</topic><topic>RNA-directed DNA polymerase</topic><topic>Spodoptera litura</topic><topic>Tobacco</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirowatari, Aiko</creatorcontrib><creatorcontrib>Chen, Zhiwei</creatorcontrib><creatorcontrib>Mita, Kazuei</creatorcontrib><creatorcontrib>Yamamoto, Kohji</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of insect biochemistry and physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hirowatari, Aiko</au><au>Chen, Zhiwei</au><au>Mita, Kazuei</au><au>Yamamoto, Kohji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura</atitle><jtitle>Archives of insect biochemistry and physiology</jtitle><addtitle>Arch Insect Biochem Physiol</addtitle><date>2018-03</date><risdate>2018</risdate><volume>97</volume><issue>3</issue><epage>n/a</epage><issn>0739-4462</issn><eissn>1520-6327</eissn><abstract>Two cDNAs encoding glutathione S‐transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase‐polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon‐class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1‐chloro‐2,4‐dinitrobenzene, 1,2‐epoxy‐3‐(4‐nitrophenoxy)‐propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29235695</pmid><doi>10.1002/arch.21443</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-5859-912X</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0739-4462 |
| ispartof | Archives of insect biochemistry and physiology, 2018-03, Vol.97 (3), p.n/a |
| issn | 0739-4462 1520-6327 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1976443485 |
| source | Wiley Online Library Journals Frontfile Complete |
| subjects | 1-Chloro-2,4-dinitrobenzene Dinitrobenzene E coli Ethacrynic acid Glutathione Glutathione transferase Homogeneity Insecticides Lepidoptera Polymerase chain reaction Proteins RNA-directed DNA polymerase Spodoptera litura Tobacco |
| title | Enzymatic characterization of two epsilon‐class glutathione S‐transferases of Spodoptera litura |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T06%3A43%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Enzymatic%20characterization%20of%20two%20epsilon%E2%80%90class%20glutathione%20S%E2%80%90transferases%20of%20Spodoptera%20litura&rft.jtitle=Archives%20of%20insect%20biochemistry%20and%20physiology&rft.au=Hirowatari,%20Aiko&rft.date=2018-03&rft.volume=97&rft.issue=3&rft.epage=n/a&rft.issn=0739-4462&rft.eissn=1520-6327&rft_id=info:doi/10.1002/arch.21443&rft_dat=%3Cproquest_cross%3E1976443485%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2001245554&rft_id=info:pmid/29235695&rfr_iscdi=true |