Image_4_Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers.JPEG (131.07 kB)
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Image_4_Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers.JPEG

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posted on 14.03.2022, 05:29 by Zhengxi Sun, Yilei Zhou, Yi Hu, Ning Jiang, Sijia Hu, Lei Li, Tao Li

Fusarium graminearum (F. graminearum) can cause huge yield reductions and contamination of grain with deoxynivalenol (DON), and thus is one of the most problematic pathogen of wheat worldwide. Although great efforts have been paid and great achievements have been made to control the pathogens, there is still a wide gap for understanding the mechanism underlying F. graminearum resistance. Plant LACCASEs (LACs) catalyze the oxidative polymerization of monolignols by reinforcing cell-wall of various cell types to provide mechanical support, xylem sap transportation, and defense against pest and pathogens. To date, little has been known about LAC genes in bread wheat and their potential roles in wheat-F. graminearum interaction. Through systematic analysis of the genome-wide homologs and transcriptomes of wheat, a total of 95 Triticum aestivum laccases (TaLACs) were identified, and 14 of them were responsive to F. graminearum challenge. 3D structure modelings of the 14 TaLAC proteins showed that only TaLAC78 contains the entire activity center for oxidation and the others lack the type 1 copper ion ligand (T1Cu). Both amino acid sequence alignment and three-dimensional reconstruction after amino acid mutation showed that the loss of T1Cu is not only related to variation of the key amino acid coordinating T1Cu, but also closely related to the flanking amino acids. Significantly differential temporal expression patterns of TaLACs suggested that their subfunctionalization might occur. Promoter array analysis indicated that the induction of TaLACs may be closely associated with salicylic acid signaling, dehydration, and low-oxygen stress under F. graminearum infection. Molecular docking simulation demonstrated that TaLACs can not only catalyze lignin as a substrate, but also interact with DON, which may be docked into the binding position of the monolignols, where the LACs recognize substrates. The current study provides clues for exploring the novel functions of TaLACs in wheat resistance to F. graminearum, and TaLACs maybe candidates for conferring a high level of resistance against F. graminearum in wheat.