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A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress

DnaJ proteins act as essential molecular chaperones in protein homeostasis and protein complex stabilization under stress conditions. The roles of a tomato (Lycopersicon esculentum) chloroplast-targeted DnaJ protein (LeCDJ1), whose expression was upregulated by treatment at 4 and 42 °C, and with hig...

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Autores principales: Kong, Fanying, Deng, Yongsheng, Zhou, Bin, Wang, Guodong, Wang, Yu, Meng, Qingwei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3883286/
https://www.ncbi.nlm.nih.gov/pubmed/24227338
http://dx.doi.org/10.1093/jxb/ert357
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author Kong, Fanying
Deng, Yongsheng
Zhou, Bin
Wang, Guodong
Wang, Yu
Meng, Qingwei
author_facet Kong, Fanying
Deng, Yongsheng
Zhou, Bin
Wang, Guodong
Wang, Yu
Meng, Qingwei
author_sort Kong, Fanying
collection PubMed
description DnaJ proteins act as essential molecular chaperones in protein homeostasis and protein complex stabilization under stress conditions. The roles of a tomato (Lycopersicon esculentum) chloroplast-targeted DnaJ protein (LeCDJ1), whose expression was upregulated by treatment at 4 and 42 °C, and with high light, NaCl, polyethylene glycol, and H(2)O(2), were investigated here using sense and antisense transgenic tomatoes. The sense plants exhibited not only higher chlorophyll content, fresh weight and net photosynthetic rate, but also lower accumulation of reactive oxygen species and membrane damage under chilling stress. Moreover, the maximal photochemistry efficiency of photosystem II (PSII) (F (v)/F (m)) and D1 protein content were higher in the sense plants and lower in the antisense plants, and the photoinhibitory quenching was lower in the sense plants and higher in the antisense plants, suggesting that the inhibition of PSII was less severe in the sense plants and more severe in the antisense plants compared with the wild type. Furthermore, the PSII protein complexes were also more stable in the sense plants. Interestingly, the sense plants treated with streptomycin (SM), an inhibitor of organellar translation, still showed higher F (v)/F (m), D1 protein content and PSII stability than the SM-untreated antisense plants. This finding suggested that the protective effect of LeCDJ1 on PSII was, at least partially, independent of D1 protein synthesis. Furthermore, chloroplast heat-shock protein 70 was identified as the partner of LeCDJ1. These results indicate that LeCDJ1 has essential functions in maintaining PSII under chilling stress.
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spelling pubmed-38832862014-01-07 A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress Kong, Fanying Deng, Yongsheng Zhou, Bin Wang, Guodong Wang, Yu Meng, Qingwei J Exp Bot Research Paper DnaJ proteins act as essential molecular chaperones in protein homeostasis and protein complex stabilization under stress conditions. The roles of a tomato (Lycopersicon esculentum) chloroplast-targeted DnaJ protein (LeCDJ1), whose expression was upregulated by treatment at 4 and 42 °C, and with high light, NaCl, polyethylene glycol, and H(2)O(2), were investigated here using sense and antisense transgenic tomatoes. The sense plants exhibited not only higher chlorophyll content, fresh weight and net photosynthetic rate, but also lower accumulation of reactive oxygen species and membrane damage under chilling stress. Moreover, the maximal photochemistry efficiency of photosystem II (PSII) (F (v)/F (m)) and D1 protein content were higher in the sense plants and lower in the antisense plants, and the photoinhibitory quenching was lower in the sense plants and higher in the antisense plants, suggesting that the inhibition of PSII was less severe in the sense plants and more severe in the antisense plants compared with the wild type. Furthermore, the PSII protein complexes were also more stable in the sense plants. Interestingly, the sense plants treated with streptomycin (SM), an inhibitor of organellar translation, still showed higher F (v)/F (m), D1 protein content and PSII stability than the SM-untreated antisense plants. This finding suggested that the protective effect of LeCDJ1 on PSII was, at least partially, independent of D1 protein synthesis. Furthermore, chloroplast heat-shock protein 70 was identified as the partner of LeCDJ1. These results indicate that LeCDJ1 has essential functions in maintaining PSII under chilling stress. Oxford University Press 2014-01 2013-11-13 /pmc/articles/PMC3883286/ /pubmed/24227338 http://dx.doi.org/10.1093/jxb/ert357 Text en © The Author 2013. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Paper
Kong, Fanying
Deng, Yongsheng
Zhou, Bin
Wang, Guodong
Wang, Yu
Meng, Qingwei
A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress
title A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress
title_full A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress
title_fullStr A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress
title_full_unstemmed A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress
title_short A chloroplast-targeted DnaJ protein contributes to maintenance of photosystem II under chilling stress
title_sort chloroplast-targeted dnaj protein contributes to maintenance of photosystem ii under chilling stress
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3883286/
https://www.ncbi.nlm.nih.gov/pubmed/24227338
http://dx.doi.org/10.1093/jxb/ert357
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