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The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis
Small heat shock proteins (sHSPs) play important roles in responses to heat stress. However, the functions of sHSPs in tea plants (Camellia sinensis) remain uncharacterized. A novel sHSP gene, designated CsHSP17.2, was isolated from tea plants. Subcellular localization analyses indicated that the Cs...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5430664/ https://www.ncbi.nlm.nih.gov/pubmed/28450727 http://dx.doi.org/10.1038/s41598-017-01407-x |
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author | Wang, Mingle Zou, Zhongwei Li, Qinghui Sun, Kang Chen, Xuan Li, Xinghui |
author_facet | Wang, Mingle Zou, Zhongwei Li, Qinghui Sun, Kang Chen, Xuan Li, Xinghui |
author_sort | Wang, Mingle |
collection | PubMed |
description | Small heat shock proteins (sHSPs) play important roles in responses to heat stress. However, the functions of sHSPs in tea plants (Camellia sinensis) remain uncharacterized. A novel sHSP gene, designated CsHSP17.2, was isolated from tea plants. Subcellular localization analyses indicated that the CsHSP17.2 protein was present in the cytosol and the nucleus. CsHSP17.2 expression was significantly up-regulated by heat stress but was unaffected by low temperature. The CsHSP17.2 transcript levels increased following salt and polyethylene glycol 6000 treatments but decreased in the presence of abscisic acid. The molecular chaperone activity of CsHSP17.2 was demonstrated in vitro. Transgenic Escherichia coli and Pichia pastoris expressing CsHSP17.2 exhibited enhanced thermotolerance. The transgenic Arabidopsis thaliana exhibited higher maximum photochemical efficiencies, greater soluble protein proline contents, higher germination rates and higher hypocotyl elongation length than the wild-type controls. The expression levels of several HS-responsive genes increased in transgenic A. thaliana plants. Additionally, the CsHSP17.2 promoter is highly responsive to high-temperature stress in A. thaliana. Our results suggest that CsHSP17.2 may act as a molecular chaperone to mediate heat tolerance by maintaining maximum photochemical efficiency and protein synthesis, enhancing the scavenging of reactive oxygen species and inducing the expression of HS-responsive genes. |
format | Online Article Text |
id | pubmed-5430664 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54306642017-05-15 The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis Wang, Mingle Zou, Zhongwei Li, Qinghui Sun, Kang Chen, Xuan Li, Xinghui Sci Rep Article Small heat shock proteins (sHSPs) play important roles in responses to heat stress. However, the functions of sHSPs in tea plants (Camellia sinensis) remain uncharacterized. A novel sHSP gene, designated CsHSP17.2, was isolated from tea plants. Subcellular localization analyses indicated that the CsHSP17.2 protein was present in the cytosol and the nucleus. CsHSP17.2 expression was significantly up-regulated by heat stress but was unaffected by low temperature. The CsHSP17.2 transcript levels increased following salt and polyethylene glycol 6000 treatments but decreased in the presence of abscisic acid. The molecular chaperone activity of CsHSP17.2 was demonstrated in vitro. Transgenic Escherichia coli and Pichia pastoris expressing CsHSP17.2 exhibited enhanced thermotolerance. The transgenic Arabidopsis thaliana exhibited higher maximum photochemical efficiencies, greater soluble protein proline contents, higher germination rates and higher hypocotyl elongation length than the wild-type controls. The expression levels of several HS-responsive genes increased in transgenic A. thaliana plants. Additionally, the CsHSP17.2 promoter is highly responsive to high-temperature stress in A. thaliana. Our results suggest that CsHSP17.2 may act as a molecular chaperone to mediate heat tolerance by maintaining maximum photochemical efficiency and protein synthesis, enhancing the scavenging of reactive oxygen species and inducing the expression of HS-responsive genes. Nature Publishing Group UK 2017-04-27 /pmc/articles/PMC5430664/ /pubmed/28450727 http://dx.doi.org/10.1038/s41598-017-01407-x Text en © The Author(s) 2017 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 Wang, Mingle Zou, Zhongwei Li, Qinghui Sun, Kang Chen, Xuan Li, Xinghui The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis |
title | The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis |
title_full | The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis |
title_fullStr | The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis |
title_full_unstemmed | The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis |
title_short | The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis |
title_sort | cshsp17.2 molecular chaperone is essential for thermotolerance in camellia sinensis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5430664/ https://www.ncbi.nlm.nih.gov/pubmed/28450727 http://dx.doi.org/10.1038/s41598-017-01407-x |
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