Identifying a sigma class glutathione S-transferase 2 from the silkworm Bombyx mori
A cDNA that encodes a sigma class glutathione S-transferase (GST; bmGSTS2) from the silkworm (Bombyx mori) was cloned by reverse transcriptase polymerase chain reaction and sequenced. The deduced amino acid sequence revealed 68%-63% identity with the sigma class GSTs from other insects. bmGSTS2 mRNA...
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| Veröffentlicht in: | Journal of Insect Biotechnology and Sericology 2017, Vol.86(1), pp.1_001-1_007 |
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| container_title | Journal of Insect Biotechnology and Sericology |
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| creator | Hirowatari, Aiko Nagaoka, Sumiharu Yamada, Naotaka Yamamoto, Kohji |
| description | A cDNA that encodes a sigma class glutathione S-transferase (GST; bmGSTS2) from the silkworm (Bombyx mori) was cloned by reverse transcriptase polymerase chain reaction and sequenced. The deduced amino acid sequence revealed 68%-63% identity with the sigma class GSTs from other insects. bmGSTS2 mRNA was widely distributed in various tissues. The recombinant enzyme was functionally overexpressed as a soluble form in Escherichia coli, purified to homogeneity, and characterized. The optimum pH of bmGSTS2 was approximately pH 7.0, and bmGSTS2 retained >75% of its original activity after incubation for 12 h at pH 6.0-8.0. Incubation for 30 min at temperatures below 40°C did not affect the enzymatic activity. bmGSTS2 was able to catalyze the reaction of glutathione with hydrogen peroxide, and 4-hydroxynonenal. These results indicate that bmGSTS2 may play a role in antioxidant defense in the silkworm. |
| doi_str_mv | 10.11416/jibs.86.1_001 |
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The deduced amino acid sequence revealed 68%-63% identity with the sigma class GSTs from other insects. bmGSTS2 mRNA was widely distributed in various tissues. The recombinant enzyme was functionally overexpressed as a soluble form in Escherichia coli, purified to homogeneity, and characterized. The optimum pH of bmGSTS2 was approximately pH 7.0, and bmGSTS2 retained >75% of its original activity after incubation for 12 h at pH 6.0-8.0. Incubation for 30 min at temperatures below 40°C did not affect the enzymatic activity. bmGSTS2 was able to catalyze the reaction of glutathione with hydrogen peroxide, and 4-hydroxynonenal. These results indicate that bmGSTS2 may play a role in antioxidant defense in the silkworm.</description><identifier>ISSN: 1346-8073</identifier><identifier>EISSN: 1884-7978</identifier><identifier>DOI: 10.11416/jibs.86.1_001</identifier><language>eng</language><publisher>Ibaraki: The Japanese Society of Sericultural Science</publisher><subject>Amino acid sequence ; Antioxidants ; Bombyx mori ; cDNA sequence ; Complementary DNA ; Defense mechanisms ; E coli ; Enzymatic activity ; Glutathione ; glutathione S-transferase ; Glutathione transferase ; Homogeneity ; Hydrogen ions ; Hydrogen peroxide ; Insects ; Polymerase chain reaction ; silkworm ; Tissues</subject><ispartof>Journal of Insect Biotechnology and Sericology, 2017, Vol.86(1), pp.1_001-1_007</ispartof><rights>2017 by Japan Academic Association for Copyright Clearance (Except in the USA), Copyright Clearance Center, Inc. (In the USA)</rights><rights>Copyright Japan Science and Technology Agency 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1881,4022,27921,27922,27923</link.rule.ids></links><search><creatorcontrib>Hirowatari, Aiko</creatorcontrib><creatorcontrib>Nagaoka, Sumiharu</creatorcontrib><creatorcontrib>Yamada, Naotaka</creatorcontrib><creatorcontrib>Yamamoto, Kohji</creatorcontrib><title>Identifying a sigma class glutathione S-transferase 2 from the silkworm Bombyx mori</title><title>Journal of Insect Biotechnology and Sericology</title><addtitle>J. Insect Biotechnol. Sericol.</addtitle><description>A cDNA that encodes a sigma class glutathione S-transferase (GST; bmGSTS2) from the silkworm (Bombyx mori) was cloned by reverse transcriptase polymerase chain reaction and sequenced. The deduced amino acid sequence revealed 68%-63% identity with the sigma class GSTs from other insects. bmGSTS2 mRNA was widely distributed in various tissues. The recombinant enzyme was functionally overexpressed as a soluble form in Escherichia coli, purified to homogeneity, and characterized. The optimum pH of bmGSTS2 was approximately pH 7.0, and bmGSTS2 retained >75% of its original activity after incubation for 12 h at pH 6.0-8.0. Incubation for 30 min at temperatures below 40°C did not affect the enzymatic activity. bmGSTS2 was able to catalyze the reaction of glutathione with hydrogen peroxide, and 4-hydroxynonenal. These results indicate that bmGSTS2 may play a role in antioxidant defense in the silkworm.</description><subject>Amino acid sequence</subject><subject>Antioxidants</subject><subject>Bombyx mori</subject><subject>cDNA sequence</subject><subject>Complementary DNA</subject><subject>Defense mechanisms</subject><subject>E coli</subject><subject>Enzymatic activity</subject><subject>Glutathione</subject><subject>glutathione S-transferase</subject><subject>Glutathione transferase</subject><subject>Homogeneity</subject><subject>Hydrogen ions</subject><subject>Hydrogen peroxide</subject><subject>Insects</subject><subject>Polymerase chain reaction</subject><subject>silkworm</subject><subject>Tissues</subject><issn>1346-8073</issn><issn>1884-7978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNo9UMtOwzAQtBBIlMKVsyXOKX7Fdm9ARaFSJQ6Fs-Wkm9QhiYvtCvr3JCrisrPSzu7ODEK3lMwoFVTeN66IMy1n1BBCz9CEai0yNVf6fOi5kJkmil-iqxgbQjjPczFBm9UW-uSqo-trbHF0dWdx2doYcd0ekk0753vAmywF28cKgo2AGa6C73DawbDQfn770OEn3xXHH9z54K7RRWXbCDd_OEUfy-f3xWu2fntZLR7XWcMYTdkgTFpG7bak5ZwTIRRUo8I8rwrGCJU5A8a2kOcaiCo4UK1IWZRzaQvBKsan6O50dx_81wFiMo0_hH54aUbrXCkpRtbDidXEZGsw--A6G47GhuTKFsyYmtHS0FMZovsflTsbDPT8F4HoaWQ</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Hirowatari, Aiko</creator><creator>Nagaoka, Sumiharu</creator><creator>Yamada, Naotaka</creator><creator>Yamamoto, Kohji</creator><general>The Japanese Society of Sericultural Science</general><general>Japan Science and Technology Agency</general><scope>7QO</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>2017</creationdate><title>Identifying a sigma class glutathione S-transferase 2 from the silkworm Bombyx mori</title><author>Hirowatari, Aiko ; Nagaoka, Sumiharu ; Yamada, Naotaka ; Yamamoto, Kohji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j221t-9786a21adc1c930447ef807355fb2201652e22de558e07b3e1870cbc96ab42f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino acid sequence</topic><topic>Antioxidants</topic><topic>Bombyx mori</topic><topic>cDNA sequence</topic><topic>Complementary DNA</topic><topic>Defense mechanisms</topic><topic>E coli</topic><topic>Enzymatic activity</topic><topic>Glutathione</topic><topic>glutathione S-transferase</topic><topic>Glutathione transferase</topic><topic>Homogeneity</topic><topic>Hydrogen ions</topic><topic>Hydrogen peroxide</topic><topic>Insects</topic><topic>Polymerase chain reaction</topic><topic>silkworm</topic><topic>Tissues</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirowatari, Aiko</creatorcontrib><creatorcontrib>Nagaoka, Sumiharu</creatorcontrib><creatorcontrib>Yamada, Naotaka</creatorcontrib><creatorcontrib>Yamamoto, Kohji</creatorcontrib><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of Insect Biotechnology and Sericology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hirowatari, Aiko</au><au>Nagaoka, Sumiharu</au><au>Yamada, Naotaka</au><au>Yamamoto, Kohji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identifying a sigma class glutathione S-transferase 2 from the silkworm Bombyx mori</atitle><jtitle>Journal of Insect Biotechnology and Sericology</jtitle><addtitle>J. Insect Biotechnol. Sericol.</addtitle><date>2017</date><risdate>2017</risdate><volume>86</volume><issue>1</issue><spage>1_001</spage><epage>1_007</epage><pages>1_001-1_007</pages><issn>1346-8073</issn><eissn>1884-7978</eissn><abstract>A cDNA that encodes a sigma class glutathione S-transferase (GST; bmGSTS2) from the silkworm (Bombyx mori) was cloned by reverse transcriptase polymerase chain reaction and sequenced. The deduced amino acid sequence revealed 68%-63% identity with the sigma class GSTs from other insects. bmGSTS2 mRNA was widely distributed in various tissues. The recombinant enzyme was functionally overexpressed as a soluble form in Escherichia coli, purified to homogeneity, and characterized. The optimum pH of bmGSTS2 was approximately pH 7.0, and bmGSTS2 retained >75% of its original activity after incubation for 12 h at pH 6.0-8.0. Incubation for 30 min at temperatures below 40°C did not affect the enzymatic activity. bmGSTS2 was able to catalyze the reaction of glutathione with hydrogen peroxide, and 4-hydroxynonenal. These results indicate that bmGSTS2 may play a role in antioxidant defense in the silkworm.</abstract><cop>Ibaraki</cop><pub>The Japanese Society of Sericultural Science</pub><doi>10.11416/jibs.86.1_001</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acid sequence Antioxidants Bombyx mori cDNA sequence Complementary DNA Defense mechanisms E coli Enzymatic activity Glutathione glutathione S-transferase Glutathione transferase Homogeneity Hydrogen ions Hydrogen peroxide Insects Polymerase chain reaction silkworm Tissues |
| title | Identifying a sigma class glutathione S-transferase 2 from the silkworm Bombyx mori |
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