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Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana

Systemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that...

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Autores principales: Zhou, Qingfeng, Meng, Qi, Tan, Xiaomin, Ding, Wei, Ma, Kang, Xu, Ziqin, Huang, Xuan, Gao, Hang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8632492/
https://www.ncbi.nlm.nih.gov/pubmed/34858456
http://dx.doi.org/10.3389/fpls.2021.748287
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author Zhou, Qingfeng
Meng, Qi
Tan, Xiaomin
Ding, Wei
Ma, Kang
Xu, Ziqin
Huang, Xuan
Gao, Hang
author_facet Zhou, Qingfeng
Meng, Qi
Tan, Xiaomin
Ding, Wei
Ma, Kang
Xu, Ziqin
Huang, Xuan
Gao, Hang
author_sort Zhou, Qingfeng
collection PubMed
description Systemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that occurs in systemic leaves of SAR-induced plants is poorly understood. We used a data-independent acquisition (DIA) phosphoproteomics platform based on high-resolution mass spectrometry in an Arabidopsis thaliana model to identify phosphoproteins related to SAR establishment. A total of 8011 phosphorylation sites from 3234 proteins were identified in systemic leaves of Pseudomonas syringae pv. maculicola ES4326 (Psm ES4326) and mock locally inoculated plants. A total of 859 significantly changed phosphoproteins from 1119 significantly changed phosphopeptides were detected in systemic leaves of Psm ES4326 locally inoculated plants, including numerous transcription factors and kinases. A variety of defense response-related proteins were found to be differentially phosphorylated in systemic leaves of Psm ES4326 locally inoculated leaves, suggesting that these proteins may be functionally involved in SAR through phosphorylation or dephosphorylation. Significantly changed phosphoproteins were enriched mainly in categories related to response to abscisic acid, regulation of stomatal movement, plant–pathogen interaction, MAPK signaling pathway, purine metabolism, photosynthesis-antenna proteins, and flavonoid biosynthesis. A total of 28 proteins were regulated at both protein and phosphorylation levels during SAR. RT-qPCR analysis revealed that changes in phosphorylation levels of proteins during SAR did not result from changes in transcript abundance. This study provides comprehensive details of key phosphoproteins associated with SAR, which will facilitate further research on the molecular mechanisms of SAR.
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spelling pubmed-86324922021-12-01 Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana Zhou, Qingfeng Meng, Qi Tan, Xiaomin Ding, Wei Ma, Kang Xu, Ziqin Huang, Xuan Gao, Hang Front Plant Sci Plant Science Systemic acquired resistance (SAR) in plants is a defense response that provides resistance against a wide range of pathogens at the whole-plant level following primary infection. Although the molecular mechanisms of SAR have been extensively studied in recent years, the role of phosphorylation that occurs in systemic leaves of SAR-induced plants is poorly understood. We used a data-independent acquisition (DIA) phosphoproteomics platform based on high-resolution mass spectrometry in an Arabidopsis thaliana model to identify phosphoproteins related to SAR establishment. A total of 8011 phosphorylation sites from 3234 proteins were identified in systemic leaves of Pseudomonas syringae pv. maculicola ES4326 (Psm ES4326) and mock locally inoculated plants. A total of 859 significantly changed phosphoproteins from 1119 significantly changed phosphopeptides were detected in systemic leaves of Psm ES4326 locally inoculated plants, including numerous transcription factors and kinases. A variety of defense response-related proteins were found to be differentially phosphorylated in systemic leaves of Psm ES4326 locally inoculated leaves, suggesting that these proteins may be functionally involved in SAR through phosphorylation or dephosphorylation. Significantly changed phosphoproteins were enriched mainly in categories related to response to abscisic acid, regulation of stomatal movement, plant–pathogen interaction, MAPK signaling pathway, purine metabolism, photosynthesis-antenna proteins, and flavonoid biosynthesis. A total of 28 proteins were regulated at both protein and phosphorylation levels during SAR. RT-qPCR analysis revealed that changes in phosphorylation levels of proteins during SAR did not result from changes in transcript abundance. This study provides comprehensive details of key phosphoproteins associated with SAR, which will facilitate further research on the molecular mechanisms of SAR. Frontiers Media S.A. 2021-11-11 /pmc/articles/PMC8632492/ /pubmed/34858456 http://dx.doi.org/10.3389/fpls.2021.748287 Text en Copyright © 2021 Zhou, Meng, Tan, Ding, Ma, Xu, Huang and Gao. 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
Zhou, Qingfeng
Meng, Qi
Tan, Xiaomin
Ding, Wei
Ma, Kang
Xu, Ziqin
Huang, Xuan
Gao, Hang
Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_full Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_fullStr Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_full_unstemmed Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_short Protein Phosphorylation Changes During Systemic Acquired Resistance in Arabidopsis thaliana
title_sort protein phosphorylation changes during systemic acquired resistance in arabidopsis thaliana
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8632492/
https://www.ncbi.nlm.nih.gov/pubmed/34858456
http://dx.doi.org/10.3389/fpls.2021.748287
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