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Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications
Ascorbate peroxidase (APX) is an important reactive oxygen species (ROS)-scavenging enzyme, which catalyzes the removal of hydrogen peroxide (H(2)O(2)) to prevent oxidative damage. The peroxidase activity of APX is regulated by posttranslational modifications (PTMs), such as S-nitrosylation, tyrosin...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8236860/ https://www.ncbi.nlm.nih.gov/pubmed/34194454 http://dx.doi.org/10.3389/fpls.2021.678111 |
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author | Kaur, Shubhpreet Prakash, Prapti Bak, Dong-Ho Hong, Sung Hyun Cho, Chuloh Chung, Moon-Soo Kim, Jin-Hong Lee, Sungbeom Bai, Hyoung-Woo Lee, Sang Yeol Chung, Byung Yeoup Lee, Seung Sik |
author_facet | Kaur, Shubhpreet Prakash, Prapti Bak, Dong-Ho Hong, Sung Hyun Cho, Chuloh Chung, Moon-Soo Kim, Jin-Hong Lee, Sungbeom Bai, Hyoung-Woo Lee, Sang Yeol Chung, Byung Yeoup Lee, Seung Sik |
author_sort | Kaur, Shubhpreet |
collection | PubMed |
description | Ascorbate peroxidase (APX) is an important reactive oxygen species (ROS)-scavenging enzyme, which catalyzes the removal of hydrogen peroxide (H(2)O(2)) to prevent oxidative damage. The peroxidase activity of APX is regulated by posttranslational modifications (PTMs), such as S-nitrosylation, tyrosine nitration, and S-sulfhydration. In addition, it has been recently reported that APX functions as a molecular chaperone, protecting rice against heat stress. In this study, we attempted to identify the various functions of APX in Arabidopsis and the effects of PTMs on these functions. Cytosol type APX1 from Arabidopsis thaliana (AtAPX1) exists in multimeric forms ranging from dimeric to high-molecular-weight (HMW) complexes. Similar to the rice APX2, AtAPX1 plays a dual role behaving both as a regular peroxidase and a chaperone molecule. The dual activity of AtAPX1 was strongly related to its structural status. The main dimeric form of the AtAPX1 protein showed the highest peroxidase activity, whereas the HMW form exhibited the highest chaperone activity. Moreover, in vivo studies indicated that the structure of AtAPX1 was regulated by heat and salt stresses, with both involved in the association and dissociation of complexes, respectively. Additionally, we investigated the effects of S-nitrosylation, S-sulfhydration, and tyrosine nitration on the protein structure and functions using gel analysis and enzymatic activity assays. S-nitrosylation and S-sulfhydration positively regulated the peroxidase activity, whereas tyrosine nitration had a negative impact. However, no effects were observed on the chaperone function and the oligomeric status of AtAPX1. Our results will facilitate the understanding of the role and regulation of APX under abiotic stress and posttranslational modifications. |
format | Online Article Text |
id | pubmed-8236860 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-82368602021-06-29 Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications Kaur, Shubhpreet Prakash, Prapti Bak, Dong-Ho Hong, Sung Hyun Cho, Chuloh Chung, Moon-Soo Kim, Jin-Hong Lee, Sungbeom Bai, Hyoung-Woo Lee, Sang Yeol Chung, Byung Yeoup Lee, Seung Sik Front Plant Sci Plant Science Ascorbate peroxidase (APX) is an important reactive oxygen species (ROS)-scavenging enzyme, which catalyzes the removal of hydrogen peroxide (H(2)O(2)) to prevent oxidative damage. The peroxidase activity of APX is regulated by posttranslational modifications (PTMs), such as S-nitrosylation, tyrosine nitration, and S-sulfhydration. In addition, it has been recently reported that APX functions as a molecular chaperone, protecting rice against heat stress. In this study, we attempted to identify the various functions of APX in Arabidopsis and the effects of PTMs on these functions. Cytosol type APX1 from Arabidopsis thaliana (AtAPX1) exists in multimeric forms ranging from dimeric to high-molecular-weight (HMW) complexes. Similar to the rice APX2, AtAPX1 plays a dual role behaving both as a regular peroxidase and a chaperone molecule. The dual activity of AtAPX1 was strongly related to its structural status. The main dimeric form of the AtAPX1 protein showed the highest peroxidase activity, whereas the HMW form exhibited the highest chaperone activity. Moreover, in vivo studies indicated that the structure of AtAPX1 was regulated by heat and salt stresses, with both involved in the association and dissociation of complexes, respectively. Additionally, we investigated the effects of S-nitrosylation, S-sulfhydration, and tyrosine nitration on the protein structure and functions using gel analysis and enzymatic activity assays. S-nitrosylation and S-sulfhydration positively regulated the peroxidase activity, whereas tyrosine nitration had a negative impact. However, no effects were observed on the chaperone function and the oligomeric status of AtAPX1. Our results will facilitate the understanding of the role and regulation of APX under abiotic stress and posttranslational modifications. Frontiers Media S.A. 2021-06-14 /pmc/articles/PMC8236860/ /pubmed/34194454 http://dx.doi.org/10.3389/fpls.2021.678111 Text en Copyright © 2021 Kaur, Prakash, Bak, Hong, Cho, Chung, Kim, Lee, Bai, Lee, Chung and Lee. 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 Kaur, Shubhpreet Prakash, Prapti Bak, Dong-Ho Hong, Sung Hyun Cho, Chuloh Chung, Moon-Soo Kim, Jin-Hong Lee, Sungbeom Bai, Hyoung-Woo Lee, Sang Yeol Chung, Byung Yeoup Lee, Seung Sik Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications |
title | Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications |
title_full | Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications |
title_fullStr | Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications |
title_full_unstemmed | Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications |
title_short | Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications |
title_sort | regulation of dual activity of ascorbate peroxidase 1 from arabidopsis thaliana by conformational changes and posttranslational modifications |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8236860/ https://www.ncbi.nlm.nih.gov/pubmed/34194454 http://dx.doi.org/10.3389/fpls.2021.678111 |
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