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CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants
Photosystem II repair in chloroplasts is a critical process involved in maintaining a plant’s photosynthetic activity under cold stress. FtsH (filamentation temperature-sensitive H) is an essential metalloprotease that is required for chloroplast photosystem II repair. However, the role of FtsH in t...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10094637/ https://www.ncbi.nlm.nih.gov/pubmed/37047263 http://dx.doi.org/10.3390/ijms24076288 |
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author | Di, Taimei Wu, Yedie Peng, Jing Wang, Jie Wang, Haoqian He, Mingming Li, Nana Hao, Xinyuan Yang, Yajun Ni, Dejiang Wang, Lu Wang, Xinchao |
author_facet | Di, Taimei Wu, Yedie Peng, Jing Wang, Jie Wang, Haoqian He, Mingming Li, Nana Hao, Xinyuan Yang, Yajun Ni, Dejiang Wang, Lu Wang, Xinchao |
author_sort | Di, Taimei |
collection | PubMed |
description | Photosystem II repair in chloroplasts is a critical process involved in maintaining a plant’s photosynthetic activity under cold stress. FtsH (filamentation temperature-sensitive H) is an essential metalloprotease that is required for chloroplast photosystem II repair. However, the role of FtsH in tea plants and its regulatory mechanism under cold stress remains elusive. In this study, we cloned a FtsH homolog gene in tea plants, named CsFtsH5, and found that CsFtsH5 was located in the chloroplast and cytomembrane. RT-qPCR showed that the expression of CsFtsH5 was increased with leaf maturity and was significantly induced by light and cold stress. Transient knockdown CsFtsH5 expression in tea leaves using antisense oligonucleotides resulted in hypersensitivity to cold stress, along with higher relative electrolyte leakage and lower Fv/Fm values. To investigate the molecular mechanism underlying CsFtsH5 involvement in the cold stress, we focused on the calcineurin B-like-interacting protein kinase 11 (CsCIPK11), which had a tissue expression pattern similar to that of CsFtsH5 and was also upregulated by light and cold stress. Yeast two-hybrid and dual luciferase (Luc) complementation assays revealed that CsFtsH5 interacted with CsCIPK11. Furthermore, the Dual-Luc assay showed that CsCIPK11-CsFtsH5 interaction might enhance CsFtsH5 stability. Altogether, our study demonstrates that CsFtsH5 is associated with CsCIPK11 and plays a positive role in maintaining the photosynthetic activity of tea plants in response to low temperatures. |
format | Online Article Text |
id | pubmed-10094637 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100946372023-04-13 CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants Di, Taimei Wu, Yedie Peng, Jing Wang, Jie Wang, Haoqian He, Mingming Li, Nana Hao, Xinyuan Yang, Yajun Ni, Dejiang Wang, Lu Wang, Xinchao Int J Mol Sci Article Photosystem II repair in chloroplasts is a critical process involved in maintaining a plant’s photosynthetic activity under cold stress. FtsH (filamentation temperature-sensitive H) is an essential metalloprotease that is required for chloroplast photosystem II repair. However, the role of FtsH in tea plants and its regulatory mechanism under cold stress remains elusive. In this study, we cloned a FtsH homolog gene in tea plants, named CsFtsH5, and found that CsFtsH5 was located in the chloroplast and cytomembrane. RT-qPCR showed that the expression of CsFtsH5 was increased with leaf maturity and was significantly induced by light and cold stress. Transient knockdown CsFtsH5 expression in tea leaves using antisense oligonucleotides resulted in hypersensitivity to cold stress, along with higher relative electrolyte leakage and lower Fv/Fm values. To investigate the molecular mechanism underlying CsFtsH5 involvement in the cold stress, we focused on the calcineurin B-like-interacting protein kinase 11 (CsCIPK11), which had a tissue expression pattern similar to that of CsFtsH5 and was also upregulated by light and cold stress. Yeast two-hybrid and dual luciferase (Luc) complementation assays revealed that CsFtsH5 interacted with CsCIPK11. Furthermore, the Dual-Luc assay showed that CsCIPK11-CsFtsH5 interaction might enhance CsFtsH5 stability. Altogether, our study demonstrates that CsFtsH5 is associated with CsCIPK11 and plays a positive role in maintaining the photosynthetic activity of tea plants in response to low temperatures. MDPI 2023-03-27 /pmc/articles/PMC10094637/ /pubmed/37047263 http://dx.doi.org/10.3390/ijms24076288 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Di, Taimei Wu, Yedie Peng, Jing Wang, Jie Wang, Haoqian He, Mingming Li, Nana Hao, Xinyuan Yang, Yajun Ni, Dejiang Wang, Lu Wang, Xinchao CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants |
title | CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants |
title_full | CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants |
title_fullStr | CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants |
title_full_unstemmed | CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants |
title_short | CsCIPK11-Regulated Metalloprotease CsFtsH5 Mediates the Cold Response of Tea Plants |
title_sort | cscipk11-regulated metalloprotease csftsh5 mediates the cold response of tea plants |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10094637/ https://www.ncbi.nlm.nih.gov/pubmed/37047263 http://dx.doi.org/10.3390/ijms24076288 |
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