The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis

Abstract 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 th...

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Autores principales:	Mingle Wang, Zhongwei Zou, Qinghui Li, Kang Sun, Xuan Chen, Xinghui Li
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ffae430940724e678997eb76320b0e01
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spelling	oai:doaj.org-article:ffae430940724e678997eb76320b0e012021-12-02T15:06:27ZThe CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis10.1038/s41598-017-01407-x2045-2322https://doaj.org/article/ffae430940724e678997eb76320b0e012017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01407-xhttps://doaj.org/toc/2045-2322Abstract 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.Mingle WangZhongwei ZouQinghui LiKang SunXuan ChenXinghui LiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mingle Wang Zhongwei Zou Qinghui Li Kang Sun Xuan Chen Xinghui Li The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis
description	Abstract 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	article
author	Mingle Wang Zhongwei Zou Qinghui Li Kang Sun Xuan Chen Xinghui Li
author_facet	Mingle Wang Zhongwei Zou Qinghui Li Kang Sun Xuan Chen Xinghui Li
author_sort	Mingle Wang
title	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_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_sort	cshsp17.2 molecular chaperone is essential for thermotolerance in camellia sinensis
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ffae430940724e678997eb76320b0e01
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The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis

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