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Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone
Ascorbate peroxidase (APX) is a class I haem-containing peroxidase, which catalyses the conversion of H(2)O(2) to H(2)O and O(2) using ascorbate as the specific electron donor. APX plays a central role in the elimination of intracellular reactive oxygen species (ROS) and protects plants from the oxi...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6003922/ https://www.ncbi.nlm.nih.gov/pubmed/29907832 http://dx.doi.org/10.1038/s41598-018-27459-1 |
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author | Hong, Sung Hyun Tripathi, Bhumi Nath Chung, Moon-Soo Cho, Chuloh Lee, Sungbeom Kim, Jin-Hong Bai, Hyoung-Woo Bae, Hyeun-Jong Cho, Jae-Young Chung, Byung Yeoup Lee, Seung Sik |
author_facet | Hong, Sung Hyun Tripathi, Bhumi Nath Chung, Moon-Soo Cho, Chuloh Lee, Sungbeom Kim, Jin-Hong Bai, Hyoung-Woo Bae, Hyeun-Jong Cho, Jae-Young Chung, Byung Yeoup Lee, Seung Sik |
author_sort | Hong, Sung Hyun |
collection | PubMed |
description | Ascorbate peroxidase (APX) is a class I haem-containing peroxidase, which catalyses the conversion of H(2)O(2) to H(2)O and O(2) using ascorbate as the specific electron donor. APX plays a central role in the elimination of intracellular reactive oxygen species (ROS) and protects plants from the oxidative damage that can occur as a result of biotic and abiotic stresses. At present, the only known function of APX is as a peroxidase. However, in this study, we demonstrate that Oryza sativa APX2 also operates as a molecular chaperone in rice. The different functions of OsAPX2 correlate strongly with its structural conformation. The high-molecular-weight (HMW) complexes had chaperone activity, whereas the low-molecular-weight (LMW) forms displayed predominantly APX activity. The APX activity was effectively inhibited by sodium azide, which is an inhibitor of haem-containing enzymes, but this did not affect the protein’s activity as a chaperone. Additionally, the OsAPX2 conformational changes could be regulated by salt and heat stresses and these stimulated OsAPX2 dissociation and association, respectively. Our results provide new insight into the roles of APXs. |
format | Online Article Text |
id | pubmed-6003922 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-60039222018-06-26 Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone Hong, Sung Hyun Tripathi, Bhumi Nath Chung, Moon-Soo Cho, Chuloh Lee, Sungbeom Kim, Jin-Hong Bai, Hyoung-Woo Bae, Hyeun-Jong Cho, Jae-Young Chung, Byung Yeoup Lee, Seung Sik Sci Rep Article Ascorbate peroxidase (APX) is a class I haem-containing peroxidase, which catalyses the conversion of H(2)O(2) to H(2)O and O(2) using ascorbate as the specific electron donor. APX plays a central role in the elimination of intracellular reactive oxygen species (ROS) and protects plants from the oxidative damage that can occur as a result of biotic and abiotic stresses. At present, the only known function of APX is as a peroxidase. However, in this study, we demonstrate that Oryza sativa APX2 also operates as a molecular chaperone in rice. The different functions of OsAPX2 correlate strongly with its structural conformation. The high-molecular-weight (HMW) complexes had chaperone activity, whereas the low-molecular-weight (LMW) forms displayed predominantly APX activity. The APX activity was effectively inhibited by sodium azide, which is an inhibitor of haem-containing enzymes, but this did not affect the protein’s activity as a chaperone. Additionally, the OsAPX2 conformational changes could be regulated by salt and heat stresses and these stimulated OsAPX2 dissociation and association, respectively. Our results provide new insight into the roles of APXs. Nature Publishing Group UK 2018-06-15 /pmc/articles/PMC6003922/ /pubmed/29907832 http://dx.doi.org/10.1038/s41598-018-27459-1 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Hong, Sung Hyun Tripathi, Bhumi Nath Chung, Moon-Soo Cho, Chuloh Lee, Sungbeom Kim, Jin-Hong Bai, Hyoung-Woo Bae, Hyeun-Jong Cho, Jae-Young Chung, Byung Yeoup Lee, Seung Sik Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone |
title | Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone |
title_full | Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone |
title_fullStr | Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone |
title_full_unstemmed | Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone |
title_short | Functional switching of ascorbate peroxidase 2 of rice (OsAPX2) between peroxidase and molecular chaperone |
title_sort | functional switching of ascorbate peroxidase 2 of rice (osapx2) between peroxidase and molecular chaperone |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6003922/ https://www.ncbi.nlm.nih.gov/pubmed/29907832 http://dx.doi.org/10.1038/s41598-018-27459-1 |
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