caa a22 4500 467900272 CHVBK 20180406152815.0 cr unu---uuuuu 170328e20060901xx s 000 0 eng 10.1007/s00299-006-0146-1 doi (NATIONALLICENCE)springer-10.1007/s00299-006-0146-1 Characterization of two Arabidopsis thaliana glutathione S -transferases [Elektronische Daten] [Eliana Nutricati, Antonio Miceli, Federica Blando, Luigi De Bellis] Glutathione S-transferases (GST) are multifunctional proteins encoded by a large gene family, divided on the basis of sequence identity into phi, tau, theta, zeta and lambda classes. The phi and tau classes are present only in plants. GSTs appear to be ubiquitous in plants and are involved in herbicide detoxification and stress response, but little is known about the precise role of GSTs in normal plant physiology and during biotic and abiotic stress response. Two cDNAs representing the two plant classes tau and phi, AtGSTF9 and AtGSTU26, were expressed in vitro and the corresponding proteins were analysed. Both GSTs were able to catalyse a glutathione conjugation to 1-chloro-2,4-dinitrobenzene (CDNB), but they were inactive as transferases towards p-nitrobenzylchloride (pNBC). AtGSTF9 showed activity towards benzyl isothiocyanate (BITC) and an activity as glutathione peroxidase with cumene hydroperoxide (CumHPO). AtGSTU26 was not active as glutathione peroxidase and towards BITC. RT-PCR analysis was used to evaluate the expression of the two genes in response to treatment with herbicides and safeners, chemicals, low and high temperature. Our results reveal that AtGSTU26 is induced by the chloroacetanilide herbicides alachlor and metolachlor and the safener benoxacor, and after exposure to low temperatures. In contrast, AtGSTF9 seems not to be influenced by the treatments employed. Springer-Verlag, 2006 Arabidopsis thaliana nationallicence Glutathione S -transferase nationallicence Stress nationallicence Nutricati Eliana Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università degli Studi di Lecce, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut Miceli Antonio Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università degli Studi di Lecce, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut Blando Federica Istituto di Scienze delle Produzioni Alimentari, CNR, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut De Bellis Luigi Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università degli Studi di Lecce, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut Plant Cell Reports Springer-Verlag 25/9(2006-09-01), 997-1005 0721-7714 25:9<997 2006 25 299 https://doi.org/10.1007/s00299-006-0146-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00299-006-0146-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Nutricati Eliana Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università degli Studi di Lecce, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut NATIONALLICENCE 700 1- Miceli Antonio Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università degli Studi di Lecce, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut NATIONALLICENCE 700 1- Blando Federica Istituto di Scienze delle Produzioni Alimentari, CNR, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut NATIONALLICENCE 700 1- De Bellis Luigi Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università degli Studi di Lecce, via Provinciale Lecce-Monteroni, 73100, Lecce, Italy aut NATIONALLICENCE 773 0- Plant Cell Reports Springer-Verlag 25/9(2006-09-01), 997-1005 0721-7714 25:9<997 2006 25 299 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer