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Redox-dependent functional switching of plant proteins accompanying with their structural changes
Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic or...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3724125/ https://www.ncbi.nlm.nih.gov/pubmed/23898340 http://dx.doi.org/10.3389/fpls.2013.00277 |
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author | Chi, Yong Hun Paeng, Seol Ki Kim, Min Ji Hwang, Gwang Yong Melencion, Sarah Mae B. Oh, Hun Taek Lee, Sang Yeol |
author_facet | Chi, Yong Hun Paeng, Seol Ki Kim, Min Ji Hwang, Gwang Yong Melencion, Sarah Mae B. Oh, Hun Taek Lee, Sang Yeol |
author_sort | Chi, Yong Hun |
collection | PubMed |
description | Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins. |
format | Online Article Text |
id | pubmed-3724125 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-37241252013-07-29 Redox-dependent functional switching of plant proteins accompanying with their structural changes Chi, Yong Hun Paeng, Seol Ki Kim, Min Ji Hwang, Gwang Yong Melencion, Sarah Mae B. Oh, Hun Taek Lee, Sang Yeol Front Plant Sci Plant Science Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins. Frontiers Media S.A. 2013-07-26 /pmc/articles/PMC3724125/ /pubmed/23898340 http://dx.doi.org/10.3389/fpls.2013.00277 Text en Copyright © Chi, Paeng, Kim, Hwang, Melencion, Oh and Lee. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc. |
spellingShingle | Plant Science Chi, Yong Hun Paeng, Seol Ki Kim, Min Ji Hwang, Gwang Yong Melencion, Sarah Mae B. Oh, Hun Taek Lee, Sang Yeol Redox-dependent functional switching of plant proteins accompanying with their structural changes |
title | Redox-dependent functional switching of plant proteins accompanying with their structural changes |
title_full | Redox-dependent functional switching of plant proteins accompanying with their structural changes |
title_fullStr | Redox-dependent functional switching of plant proteins accompanying with their structural changes |
title_full_unstemmed | Redox-dependent functional switching of plant proteins accompanying with their structural changes |
title_short | Redox-dependent functional switching of plant proteins accompanying with their structural changes |
title_sort | redox-dependent functional switching of plant proteins accompanying with their structural changes |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3724125/ https://www.ncbi.nlm.nih.gov/pubmed/23898340 http://dx.doi.org/10.3389/fpls.2013.00277 |
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