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A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean

Light is required for initiating chloroplast biogenesis and photosynthesis; however, the photosystem II reaction center (PSII RC) can be photodamaged. In this study, we characterized pvsl1, a seedling-lethal mutant of Phaseolus vulgaris. This mutant showed lethality when exposed to sunlight irradiat...

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Autores principales: Xu, Kun, Zhu, Jinlong, Zhai, Hong, Wu, Hongyan, Gao, Yi, Li, Yuzhuo, Zhu, Xiaobin, Xia, Zhengjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8167180/
https://www.ncbi.nlm.nih.gov/pubmed/34059658
http://dx.doi.org/10.1038/s41438-021-00554-7
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author Xu, Kun
Zhu, Jinlong
Zhai, Hong
Wu, Hongyan
Gao, Yi
Li, Yuzhuo
Zhu, Xiaobin
Xia, Zhengjun
author_facet Xu, Kun
Zhu, Jinlong
Zhai, Hong
Wu, Hongyan
Gao, Yi
Li, Yuzhuo
Zhu, Xiaobin
Xia, Zhengjun
author_sort Xu, Kun
collection PubMed
description Light is required for initiating chloroplast biogenesis and photosynthesis; however, the photosystem II reaction center (PSII RC) can be photodamaged. In this study, we characterized pvsl1, a seedling-lethal mutant of Phaseolus vulgaris. This mutant showed lethality when exposed to sunlight irradiation and a yellow-green leaf phenotype when grown in a growth chamber under low-light conditions. We developed 124 insertion/deletion (INDEL) markers based on resequencing data of Dalong1 and PI60234, two local Chinese common bean cultivars, for genetic mapping. We identified Phvul.002G190900, which encodes the PvFtsH2 protein, as the candidate gene for this pvsl1 mutation through fine-mapping and functional analysis. A single-base deletion occurred in the coding region of Phvul.002G190900 in the pvsl1 mutant, resulting in a frameshift mutation and a truncated protein lacking the Zn(2+) metalloprotease domain. Suppressed expression of Phvul.002G190900 at the transcriptional level was detected, while no change in the subcellular localization signal was observed. The seedlings of pvsl1 exhibited hypersensitivity to photoinhibition stress. In the pvsl1 mutant, abnormal accumulation of the D1 protein indicated a failure to rapidly degrade damaged D1 protein in the PSII RC. The results of this study demonstrated that PvFtsH2 is critically required for survival and maintaining photosynthetic activity by degrading photodamaged PSII RC D1 protein in common bean.
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spelling pubmed-81671802021-06-07 A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean Xu, Kun Zhu, Jinlong Zhai, Hong Wu, Hongyan Gao, Yi Li, Yuzhuo Zhu, Xiaobin Xia, Zhengjun Hortic Res Article Light is required for initiating chloroplast biogenesis and photosynthesis; however, the photosystem II reaction center (PSII RC) can be photodamaged. In this study, we characterized pvsl1, a seedling-lethal mutant of Phaseolus vulgaris. This mutant showed lethality when exposed to sunlight irradiation and a yellow-green leaf phenotype when grown in a growth chamber under low-light conditions. We developed 124 insertion/deletion (INDEL) markers based on resequencing data of Dalong1 and PI60234, two local Chinese common bean cultivars, for genetic mapping. We identified Phvul.002G190900, which encodes the PvFtsH2 protein, as the candidate gene for this pvsl1 mutation through fine-mapping and functional analysis. A single-base deletion occurred in the coding region of Phvul.002G190900 in the pvsl1 mutant, resulting in a frameshift mutation and a truncated protein lacking the Zn(2+) metalloprotease domain. Suppressed expression of Phvul.002G190900 at the transcriptional level was detected, while no change in the subcellular localization signal was observed. The seedlings of pvsl1 exhibited hypersensitivity to photoinhibition stress. In the pvsl1 mutant, abnormal accumulation of the D1 protein indicated a failure to rapidly degrade damaged D1 protein in the PSII RC. The results of this study demonstrated that PvFtsH2 is critically required for survival and maintaining photosynthetic activity by degrading photodamaged PSII RC D1 protein in common bean. Nature Publishing Group UK 2021-06-01 /pmc/articles/PMC8167180/ /pubmed/34059658 http://dx.doi.org/10.1038/s41438-021-00554-7 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Xu, Kun
Zhu, Jinlong
Zhai, Hong
Wu, Hongyan
Gao, Yi
Li, Yuzhuo
Zhu, Xiaobin
Xia, Zhengjun
A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean
title A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean
title_full A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean
title_fullStr A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean
title_full_unstemmed A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean
title_short A critical role of PvFtsH2 in the degradation of photodamaged D1 protein in common bean
title_sort critical role of pvftsh2 in the degradation of photodamaged d1 protein in common bean
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8167180/
https://www.ncbi.nlm.nih.gov/pubmed/34059658
http://dx.doi.org/10.1038/s41438-021-00554-7
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