Gst, DmGST1, gstD, DmGSTD1, GST-1
Gene model reviewed during 5.53
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\GstD1 using the Feature Mapper tool.
Comment: reported as dorsal/lateral sensory complexes
GBrowse - Visual display of RNA-Seq signalsView Dmel\GstD1 in GBrowse 2
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Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Quantifying rates of protein sequence divergence within and between species reveals that the Drosophila genome harbors a substantial proportion of genes with a very high divergence rate.
mRNA levels for GST do not increase at adult day 5 in strain showing extended longevity phenotype (ELP).
Glutathione S transferase activity has been analysed in various developmental stages.
Pentobarbital rapidly induces the expression of GstD1, by activating transcription.
Dehydro-chlorinase activity of the protein is determined by biochemical analysis using gas-liquid chromatography to assess the contribution of the isozymes to the DDT-resistant phenotype.
Encodes glutathione S transferase subunit 1 (Toung et al., Biochem. biophys. Res. Commun. 178: 1205--1211, Toung and Tu, Biochem. biophys. Res. Commun. 182: 355--360).
GstD1 locus is flanked by two clusters of heat shock genes. Enzyme activity in Kco cells is elevated slightly to two fold under heat shock.
The GstD1 gene function has been implicated in repairing cellular damage inflicted by oxygen free radicals.
Glutathione S-transferase enzyme has been purified and characterised.
Glutathione S-transferase activity shows differences in age dependence, substrate selectivity and subcellular location in adult Drosophila, suggesting the presence of multiple forms of the enzyme. Differences in activity between different Drosophila strains are also seen.
Substrate specificities and pH optima suggest that GstD1 enzyme has a restricted range of substrates. Pentamethyl benzene (PMB) causes a 50% increase in enzyme activity, whereas β,naphthoflavone and phenobarbital have no effect. The degree of response to PMB is modulated by other genes on chromosome 2. Response of enzyme activity to 1-chloro-2,3-dinitrobenzene (CDNB) and ethacrynic acid (EA) can also differ.
GstD1 gene product does not conjugate the epoxides styrene-7,8-oxide and 1,2-epoxy-3-propane.