Identification of a putative kinase interacting domain in the durum wheat catalase 1 (TdCAT1) protein.

ABSTRACT: Catalases are crucial antioxidant enzymes that regulate plants responses to different biotic and abiotic stresses. It has been previously shown that the activities of durum wheat catalase proteins (TdCAT1) were stimulated in the presence of divalent cations Mn²⁺, Mg²⁺, Fe²⁺, Zn²⁺, and Ca²⁺. In addition, TdCAT1s can interact with calmodulins in calcium-independent manner, and this interaction stimulates its catalytic activity in a calcium-dependent manner. Moreover, this activity is further enhanced by Mn²⁺ cations. The current study showed that wheat catalase presents different phosphorylation targets. Besides, we demonstrated that catalase is able to interact with Mitogen Activated Proteins kinases via a conserved domain. T

SUBMITTER: Ghorbel M 

PROVIDER: S-EPMC10440534 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature