Abstract
Glutathione S-transferases (GSTs) with additional activities as fatty acid hydroperoxidases were investigated in soybean (Glycine max L.) hypocotyls. Aside from the GSTs present in total soluble tissue extracts, enzyme activities and distinct immunoreactive GST polypeptides were also detected in the intercellular washing fluid. Whereas the intracellular isoenzymes were both constitutive and inducible, apoplastic GST and glutathione peroxidase was detectable only in tissues treated with the known GST inducer 2,3,5-triiodobenzoic acid. Monensin inhibited the induced accumulation of apoplastic GST but did not affect the intracellular isoforms. The discovery of apoplastic inducible GST will be discussed in light of the putative function of these enzymes in plants.
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- Bartling D., Radzio R., Steiner U., Weiler E. W. A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization. Eur J Biochem. 1993 Sep 1;216(2):579–586. doi: 10.1111/j.1432-1033.1993.tb18177.x. [DOI] [PubMed] [Google Scholar]
- Berhane K., Widersten M., Engström A., Kozarich J. W., Mannervik B. Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc Natl Acad Sci U S A. 1994 Feb 15;91(4):1480–1484. doi: 10.1073/pnas.91.4.1480. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brophy P. M., Patterson L. H., Brown A., Pritchard D. I. Glutathione S-transferase (GST) expression in the human hookworm Necator americanus: potential roles for excretory-secretory forms of GST. Acta Trop. 1995 Jun;59(3):259–263. doi: 10.1016/0001-706x(95)00084-r. [DOI] [PubMed] [Google Scholar]
- Droog F. N., Hooykaas P. J., Libbenga K. R., van der Zaal E. J. Proteins encoded by an auxin-regulated gene family of tobacco share limited but significant homology with glutathione S-transferases and one member indeed shows in vitro GST activity. Plant Mol Biol. 1993 Mar;21(6):965–972. doi: 10.1007/BF00023595. [DOI] [PubMed] [Google Scholar]
- Dudler R., Hertig C., Rebmann G., Bull J., Mauch F. A pathogen-induced wheat gene encodes a protein homologous to glutathione-S-transferases. Mol Plant Microbe Interact. 1991 Jan-Feb;4(1):14–18. doi: 10.1094/mpmi-4-014. [DOI] [PubMed] [Google Scholar]
- Fuerst E. P., Irzyk G. P., Miller K. D. Partial Characterization of Glutathione S-Transferase Isozymes Induced by the Herbicide Safener Benoxacor in Maize. Plant Physiol. 1993 Jul;102(3):795–802. doi: 10.1104/pp.102.3.795. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hahn K., Strittmatter G. Pathogen-defence gene prp1-1 from potato encodes an auxin-responsive glutathione S-transferase. Eur J Biochem. 1994 Dec 1;226(2):619–626. doi: 10.1111/j.1432-1033.1994.tb20088.x. [DOI] [PubMed] [Google Scholar]
- Jamai A., Tommasini R., Martinoia E., Delrot S. Characterization of Glutathione Uptake in Broad Bean Leaf Protoplasts. Plant Physiol. 1996 Aug;111(4):1145–1152. doi: 10.1104/pp.111.4.1145. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jepson I., Lay V. J., Holt D. C., Bright S. W., Greenland A. J. Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV. Plant Mol Biol. 1994 Dec;26(6):1855–1866. doi: 10.1007/BF00019498. [DOI] [PubMed] [Google Scholar]
- Kreuz K., Tommasini R., Martinoia E. Old Enzymes for a New Job (Herbicide Detoxification in Plants). Plant Physiol. 1996 Jun;111(2):349–353. doi: 10.1104/pp.111.2.349. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Mollenhauer H. H., Morré D. J., Rowe L. D. Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity. Biochim Biophys Acta. 1990 May 7;1031(2):225–246. doi: 10.1016/0304-4157(90)90008-Z. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
- Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R., Palme K., Schell J., Koelln I., Bartunik H. D. Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J Mol Biol. 1996 Jan 19;255(2):289–309. doi: 10.1006/jmbi.1996.0024. [DOI] [PubMed] [Google Scholar]
- Simmons T. W., Jamall I. S., Lockshin R. A. Selenium-independent glutathione peroxidase activity associated with glutathione S-transferase from the housefly, Musca domestica. Comp Biochem Physiol B. 1989;94(2):323–327. doi: 10.1016/0305-0491(89)90350-7. [DOI] [PubMed] [Google Scholar]
- Tenhaken R., Levine A., Brisson L. F., Dixon R. A., Lamb C. Function of the oxidative burst in hypersensitive disease resistance. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4158–4163. doi: 10.1073/pnas.92.10.4158. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ulmasov T., Ohmiya A., Hagen G., Guilfoyle T. The soybean GH2/4 gene that encodes a glutathione S-transferase has a promoter that is activated by a wide range of chemical agents. Plant Physiol. 1995 Jul;108(3):919–927. doi: 10.1104/pp.108.3.919. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wilce M. C., Parker M. W. Structure and function of glutathione S-transferases. Biochim Biophys Acta. 1994 Mar 16;1205(1):1–18. doi: 10.1016/0167-4838(94)90086-8. [DOI] [PubMed] [Google Scholar]