Abstract
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.
Highlights
Glutathione S-transferases (GSTs; E.C.2.5.1.18) are conserved enzymes that are widespread in both prokaryotes and eukaryotes
Bmgstd4 was cloned from total male silkmoth antenna RNA by 5'- and 3'-rapid amplification of cDNA ends (RACE)-PCR
BLAST of the putative conserved domains showed that BmGSTD4 was a typical GST in the δ class with an N-terminal GSH binding site and a C-terminal hydrophobic substrate-binding site
Summary
Glutathione S-transferases (GSTs; E.C.2.5.1.18) are conserved enzymes that are widespread in both prokaryotes and eukaryotes. GSTs are phase II enzymes in the detoxification and metabolism of toxic compounds [1,2,3] that catalyze xenobiotic and endobiotic compound detoxification by conjugation with reduced glutathione (GSH). This process results in water soluble, less toxic conjugates that can be excreted. Some GSTs noncatalytically bind endogenous and exogenous ligands [6,7,8]. Based on the nomenclature of the mammalian cytosolic GSTs [9], insect cytosolic
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