Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution

Two glutathione S-transferase (GST) cDNAs, GSTD2 and GSTS2, were cloned from the silkworm Bombyx mori. The B. mori GSTD2 (BmGSTD2) gene spans 4371 bp and consists of four introns and five exons that encode 222 amino acid residues. The deduced amino acid sequence of BmGSTD2 showed 58% protein sequenc...

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Main Authors: Zhong Zheng GUI, Bo Yeon KIM, Kwang Sik LEE, Ya Dong WEI, Xijie GUO, Hung Dae SOHN, Byung Rae JIN
Format: Article
Language:English
Published: Institute of Entomology, Biology Centre, Czech Academy of Science 2008-10-01
Series:European Journal of Entomology
Subjects:
Online Access:https://www.eje.cz/artkey/eje-200804-0004_Glutathione_S-transferases_from_the_larval_gut_of_the_silkworm_Bombyx_mori_cDNA_cloning_gene_structure_expre.php
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author Zhong Zheng GUI
Bo Yeon KIM
Kwang Sik LEE
Ya Dong WEI
Xijie GUO
Hung Dae SOHN
Byung Rae JIN
author_facet Zhong Zheng GUI
Bo Yeon KIM
Kwang Sik LEE
Ya Dong WEI
Xijie GUO
Hung Dae SOHN
Byung Rae JIN
author_sort Zhong Zheng GUI
collection DOAJ
description Two glutathione S-transferase (GST) cDNAs, GSTD2 and GSTS2, were cloned from the silkworm Bombyx mori. The B. mori GSTD2 (BmGSTD2) gene spans 4371 bp and consists of four introns and five exons that encode 222 amino acid residues. The deduced amino acid sequence of BmGSTD2 showed 58% protein sequence identity to the Delta-class GST of Maduca sexta. The B. mori GSTS2 (BmGSTS2) gene spans 3470 bp and consists of three introns and four exons that encode 206 amino acid residues. The deduced amino acid sequence of BmGSTS2 revealed 67%, 63%, and 61% protein sequence identities to the Sigma-class GSTs from B. mori, Platynota idaeusalis, and M. sexta, respectively. The BmGSTD2 and BmGSTS2 cDNAs were expressed as 25 kDa and 23 kDa polypeptides, respectively, in baculovirus-infected insect Sf9 cells. Northern blot and Western blot analyses showed that BmGSTD2 and BmGSTS2 were specifically expressed in three gut regions, indicating that the gut is the prime site for BmGSTD2 and BmGSTS2 synthesis in B. mori larvae.
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spelling doaj.art-d9648eabc01c471787f2132383d7949b2022-12-21T22:05:48ZengInstitute of Entomology, Biology Centre, Czech Academy of ScienceEuropean Journal of Entomology1210-57591802-88292008-10-01105456757410.14411/eje.2008.076eje-200804-0004Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distributionZhong Zheng GUI0Bo Yeon KIM1Kwang Sik LEE2Ya Dong WEI3Xijie GUO4Hung Dae SOHN5Byung Rae JIN6College of Natural Resources and Life Science, Dong-A University, Busan 604-714, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 604-714, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 604-714, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 604-714, KoreaSericultural Research Institute, Chinese Academy of Agricultural Sciences, Zhenjiang 212018, ChinaCollege of Natural Resources and Life Science, Dong-A University, Busan 604-714, KoreaCollege of Natural Resources and Life Science, Dong-A University, Busan 604-714, KoreaTwo glutathione S-transferase (GST) cDNAs, GSTD2 and GSTS2, were cloned from the silkworm Bombyx mori. The B. mori GSTD2 (BmGSTD2) gene spans 4371 bp and consists of four introns and five exons that encode 222 amino acid residues. The deduced amino acid sequence of BmGSTD2 showed 58% protein sequence identity to the Delta-class GST of Maduca sexta. The B. mori GSTS2 (BmGSTS2) gene spans 3470 bp and consists of three introns and four exons that encode 206 amino acid residues. The deduced amino acid sequence of BmGSTS2 revealed 67%, 63%, and 61% protein sequence identities to the Sigma-class GSTs from B. mori, Platynota idaeusalis, and M. sexta, respectively. The BmGSTD2 and BmGSTS2 cDNAs were expressed as 25 kDa and 23 kDa polypeptides, respectively, in baculovirus-infected insect Sf9 cells. Northern blot and Western blot analyses showed that BmGSTD2 and BmGSTS2 were specifically expressed in three gut regions, indicating that the gut is the prime site for BmGSTD2 and BmGSTS2 synthesis in B. mori larvae.https://www.eje.cz/artkey/eje-200804-0004_Glutathione_S-transferases_from_the_larval_gut_of_the_silkworm_Bombyx_mori_cDNA_cloning_gene_structure_expre.phpbaculovirus expression vectorbombyx moricdna cloningenzymegene structureglutathione s-transferasesilkworm
spellingShingle Zhong Zheng GUI
Bo Yeon KIM
Kwang Sik LEE
Ya Dong WEI
Xijie GUO
Hung Dae SOHN
Byung Rae JIN
Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution
European Journal of Entomology
baculovirus expression vector
bombyx mori
cdna cloning
enzyme
gene structure
glutathione s-transferase
silkworm
title Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution
title_full Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution
title_fullStr Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution
title_full_unstemmed Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution
title_short Glutathione S-transferases from the larval gut of the silkworm Bombyx mori: cDNA cloning, gene structure, expression and distribution
title_sort glutathione s transferases from the larval gut of the silkworm bombyx mori cdna cloning gene structure expression and distribution
topic baculovirus expression vector
bombyx mori
cdna cloning
enzyme
gene structure
glutathione s-transferase
silkworm
url https://www.eje.cz/artkey/eje-200804-0004_Glutathione_S-transferases_from_the_larval_gut_of_the_silkworm_Bombyx_mori_cDNA_cloning_gene_structure_expre.php
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