RRC ID 11048
著者 Yamamoto K, Ichinose H, Aso Y, Banno Y, Kimura M, Nakashima T.
タイトル Molecular characterization of an insecticide-induced novel glutathione transferase in silkworm.
ジャーナル Biochim Biophys Acta
Abstract BACKGROUND:The glutathione transferase (GST) superfamily is involved in the detoxification of various xenobiotics. We have identified a GST mRNA that was induced in the fat bodies of a silkworm strain exhibiting diazinon resistance and have investigated the enzyme properties of this GST.
METHODS:A soluble recombinant protein was overexpressed in Escherichia coli. Amino acid residues of interest were changed to alanine by site-directed mutagenesis.
RESULTS AND CONCLUSIONS:Phylogenetic analysis of the deduced amino acid sequence indicates that this GST belongs to an unclassified group previously reported in mosquitoes. This enzyme, named bmGSTu, has highly conserved amino acid residues, including Tyr7, Ser12 and Asn50. A recombinant bmGSTu was able to catalyze the biotranslation of glutathione with 1-chloro-2,4-dinitrobenzene, a synthetic substrate of GST. Kinetic analysis of bmGSTu mutants indicated that Tyr7, Ser12 and Asn50 are involved in enzyme function.
GENERAL SIGNIFICANCE:These results support the hypothesis that bmGSTu may play a role in insecticide resistance in Bombyx mori.
巻・号 1810(4)
ページ 420-6
公開日 2011-4-1
DOI 10.1016/j.bbagen.2011.01.003
PII S0304-4165(11)00006-7
PMID 21237249
MeSH Amino Acid Sequence Animals Bombyx / drug effects Bombyx / enzymology* Bombyx / genetics Escherichia coli / genetics Gene Expression Glutathione Transferase / genetics Glutathione Transferase / metabolism* Insecticide Resistance Insecticides / pharmacology* Molecular Sequence Data Mutagenesis, Site-Directed Phylogeny Recombinant Proteins / genetics Recombinant Proteins / metabolism Sequence Alignment
IF 3.411
引用数 24
WOS 分野 BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
カイコ NA