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Int. J. Mol. Sci. 2014, 15(5), 7429-7443; doi:10.3390/ijms15057429

Antenna-Specific Glutathione S-Transferase in Male Silkmoth Bombyx mori

1 State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China 2 Medicine Research Center, North Sichuan Medical College, Nanchong 637000, Sichuan, China
* Author to whom correspondence should be addressed.
Received: 21 January 2014 / Revised: 14 April 2014 / Accepted: 16 April 2014 / Published: 29 April 2014
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Glutathione S-transferases (GSTs) are multifunctional enzymes that are widely distributed in different species. GSTs detoxify exogenous and endogenous substances by conjugation to reduced glutathione. We characterized BmGSTD4, an antenna-specific GST, in male silkmoths. The full-length mRNA of Bmgstd4 was cloned by RACE-PCR and contained an open reading frame of 738 bp encoding a 245 amino acid protein. The antenna specificity of BmGSTD4 was validated at the mRNA and protein levels and BmGSTD4 was shown to localize in the sensillum of male silkmoth antennae. Homology modeling and multi-sequence alignment suggested that BmGSTD4 was a typical GST belonging to the δ class and had a canonical GST fold with a conserved N-terminus, including a glutathione-binding site and a C-terminal domain harboring a hydrophobic substrate-binding site. Restricted expression of BmGSTD4 in silkmoth antennae combined with GST activity suggested that BmGSTD4 was involved in the detoxification of harmful chemicals.
Keywords: glutathione S-transferase; antenna-specific; male silkmoth; detoxification; Bombyx mori glutathione S-transferase; antenna-specific; male silkmoth; detoxification; Bombyx mori
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Tan, X.; Hu, X.-M.; Zhong, X.-W.; Chen, Q.-M.; Xia, Q.-Y.; Zhao, P. Antenna-Specific Glutathione S-Transferase in Male Silkmoth Bombyx mori. Int. J. Mol. Sci. 2014, 15, 7429-7443.

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