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Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers

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...

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Autores principales: Sun, Zhengxi, Zhou, Yilei, Hu, Yi, Jiang, Ning, Hu, Sijia, Li, Lei, Li, Tao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8964265/
https://www.ncbi.nlm.nih.gov/pubmed/35360333
http://dx.doi.org/10.3389/fpls.2022.832800
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author Sun, Zhengxi
Zhou, Yilei
Hu, Yi
Jiang, Ning
Hu, Sijia
Li, Lei
Li, Tao
author_facet Sun, Zhengxi
Zhou, Yilei
Hu, Yi
Jiang, Ning
Hu, Sijia
Li, Lei
Li, Tao
author_sort Sun, Zhengxi
collection PubMed
description 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.
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spelling pubmed-89642652022-03-30 Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers Sun, Zhengxi Zhou, Yilei Hu, Yi Jiang, Ning Hu, Sijia Li, Lei Li, Tao Front Plant Sci Plant Science 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. Frontiers Media S.A. 2022-03-14 /pmc/articles/PMC8964265/ /pubmed/35360333 http://dx.doi.org/10.3389/fpls.2022.832800 Text en Copyright © 2022 Sun, Zhou, Hu, Jiang, Hu, Li and Li. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Sun, Zhengxi
Zhou, Yilei
Hu, Yi
Jiang, Ning
Hu, Sijia
Li, Lei
Li, Tao
Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers
title Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers
title_full Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers
title_fullStr Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers
title_full_unstemmed Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers
title_short Identification of Wheat LACCASEs in Response to Fusarium graminearum as Potential Deoxynivalenol Trappers
title_sort identification of wheat laccases in response to fusarium graminearum as potential deoxynivalenol trappers
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8964265/
https://www.ncbi.nlm.nih.gov/pubmed/35360333
http://dx.doi.org/10.3389/fpls.2022.832800
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