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LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce
High temperatures have significant impacts on heat-tolerant bolting in lettuce. In this study, it was found that high temperatures could facilitate the accumulation of GA in lettuce to induce bolting, with higher expression levels of two heat shock protein genes LsHsp70-3701 and LsHsp70-2711. By app...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7495476/ https://www.ncbi.nlm.nih.gov/pubmed/32939023 http://dx.doi.org/10.1038/s41598-020-72443-3 |
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author | Liu, Ran Su, Zhenqi Zhou, Huiyan Huang, Qian Fan, Shuangxi Liu, Chaojie Han, Yingyan |
author_facet | Liu, Ran Su, Zhenqi Zhou, Huiyan Huang, Qian Fan, Shuangxi Liu, Chaojie Han, Yingyan |
author_sort | Liu, Ran |
collection | PubMed |
description | High temperatures have significant impacts on heat-tolerant bolting in lettuce. In this study, it was found that high temperatures could facilitate the accumulation of GA in lettuce to induce bolting, with higher expression levels of two heat shock protein genes LsHsp70-3701 and LsHsp70-2711. By applying VIGS technology, these two Hsp70 genes were incompletely silenced and plant morphological changes under heat treatment of silenced plants were observed. The results showed that lower expression levels of these two genes could enhance bolting stem length of lettuce under high temperatures, which means these two proteins may play a significant role in heat-induced bolting tolerance. By using the yeast two-hybrid technique, it was found that a calmodulin protein could interact with LsHsp70 proteins in a high-temperature stress cDNA library, which was constructed for lettuce. Also, the Hsp70-calmodulin combination can be obtained at high temperatures. According to these results, it can be speculated that the interaction between Hsp70 and calmodulin could be induced under high temperatures and higher GA contents can be obtained at the same time. This study analyses the regulation of heat tolerance in lettuce and lays a foundation for additional studies of heat resistance in lettuce. |
format | Online Article Text |
id | pubmed-7495476 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-74954762020-09-18 LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce Liu, Ran Su, Zhenqi Zhou, Huiyan Huang, Qian Fan, Shuangxi Liu, Chaojie Han, Yingyan Sci Rep Article High temperatures have significant impacts on heat-tolerant bolting in lettuce. In this study, it was found that high temperatures could facilitate the accumulation of GA in lettuce to induce bolting, with higher expression levels of two heat shock protein genes LsHsp70-3701 and LsHsp70-2711. By applying VIGS technology, these two Hsp70 genes were incompletely silenced and plant morphological changes under heat treatment of silenced plants were observed. The results showed that lower expression levels of these two genes could enhance bolting stem length of lettuce under high temperatures, which means these two proteins may play a significant role in heat-induced bolting tolerance. By using the yeast two-hybrid technique, it was found that a calmodulin protein could interact with LsHsp70 proteins in a high-temperature stress cDNA library, which was constructed for lettuce. Also, the Hsp70-calmodulin combination can be obtained at high temperatures. According to these results, it can be speculated that the interaction between Hsp70 and calmodulin could be induced under high temperatures and higher GA contents can be obtained at the same time. This study analyses the regulation of heat tolerance in lettuce and lays a foundation for additional studies of heat resistance in lettuce. Nature Publishing Group UK 2020-09-16 /pmc/articles/PMC7495476/ /pubmed/32939023 http://dx.doi.org/10.1038/s41598-020-72443-3 Text en © The Author(s) 2020 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Liu, Ran Su, Zhenqi Zhou, Huiyan Huang, Qian Fan, Shuangxi Liu, Chaojie Han, Yingyan LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
title | LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
title_full | LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
title_fullStr | LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
title_full_unstemmed | LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
title_short | LsHSP70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
title_sort | lshsp70 is induced by high temperature to interact with calmodulin, leading to higher bolting resistance in lettuce |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7495476/ https://www.ncbi.nlm.nih.gov/pubmed/32939023 http://dx.doi.org/10.1038/s41598-020-72443-3 |
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