The Activity of the Durum Wheat (Triticum durum L.) Catalase 1 (TdCAT1) Is Modulated by Calmodulin

Antioxidants - Tập 11 Số 8 - Trang 1483
Mouna Ghorbel1,2, Kaouthar Feki3, Sana Tounsi2, Najla Haddaji1, Moez Hanin4, Faïçal Brini2
1Biology Department, Faculty of Science, University of Hail, Hai'l P.O. Box 2440, Saudi Arabia
2Laboratory of Biotechnology and Plant Improvement, Center of Biotechnology of Sfax, P.O. Box 1177, Sfax, 3018, Tunisia
3Laboratory of Legumes and Sustainable Agrostems (L2AD), Center of Biotechnology of Bordj Cedria, P.O. Box 901, Hammam Lif 2050, Tunisia
4Unité de Génomique Fonctionnelle et Physiologie des Plantes, Département de Biologie, Institut Supérieur de Biotechnologie, Université de Sfax, BP "1175", Sfax 3038, Tunisia

Tóm tắt

Plant catalases (CAT) are involved in the cellular scavenging of the reactive oxygen species during developmental processes and in response to abiotic and biotic stresses. However, little is known about the regulation of the CAT activity to ensure efficient antioxidant function. Using bioinformatic analyses, we showed that durum wheat catalase 1 (TdCAT1) harbors highly conserved cation-binding and calmodulin binding (CaMBD) domains which are localized at different positions of the protein. As a result, the catalytic activity of TdCAT1 is enhanced in vitro by the divalent cations Mn2+ and Fe2+ and to a lesser extent by Cu2+, Zn2+, and Mg2+. Moreover, the GST-pull down assays performed here revealed that TdCAT1 bind to the wheat CaM (TdCaM1.3) in a Ca2+-independent manner. Furthermore, the TdCaM1.3/Ca2+ complex is stimulated in a CaM-dose-dependent manner by the catalytic activity of TdCAT1, which is further increased in the presence of Mn2+ cations. The catalase activity of TdCAT1 is enhanced by various divalent cations and TdCaM1.3 in a Ca-dependent manner. Such effects are not reported so far and raise a possible role of CaM and cations in the function of CATs during cellular response to oxidative stress.

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