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The soybean GH2/4 gene that encodes a glutathione S-transferase has a promoter that is activated by a wide range ofchemical agents

Ulmasov, T., Ohmiya, A., Hagen, G., Guilfoyle, T.
Plant physiology 1995 v.108 no.3 pp. 919-927
heavy metals, developmental stages, cytosol, 2,4,5-T, benzene, 2,4-D, promoter regions, dose response, immunoassays, glutathione transferase, antibodies, gene expression, Nicotiana tabacum, naphthaleneacetic acid, messenger RNA, Glycine max, genetic code, transcription (genetics), enzyme activity, histochemistry, gene transfer, transgenic plants, reporter genes, protein content, beta-glucuronidase
Transcriptional activation of the soybean (Glycine max) GH2/4 gene (also referred to as Gmhsp26-A) and increase in abundance of the GH2/4 mRNA (also referred to as pCE54) have been previously shown to occur following treatment of soybean seedlings with auxins, nonauxin analogs, heavy metals, and a variety of other agents. To determine whether the GH2/4 promoter is responsive to an array of different agents, we have analyzed the inducibility of the GH2/4 promoter of to the beta-glucuronidase reporter gene in transgenic tobacco (Nicotiana tabacum) plants. We have shown that a wide variety of chemical agents induce this promoter in a tissue-specific and concentration-dependent manner. In addition, we have an affinity-purified antibody raised against recombinant GH2/4 protein to show that the GH2/4 protein increases in response to auxin application and is localized in the cytosol of soybean cells. Recombinant GH2/4 protein can be purified to homogeneity on a glutathione-agarose resin, and the purified protein has glutathione S-transferase activity when assayed with the substrate 1-chloro-2,4-dinitrobenzene.