Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress
Chloroplasts are considered to be devoid of cysteine proteases. Using transgenic Arabidopsis lines expressing the rice cystatin, oryzacystatin I (OC-I), in the chloroplasts (PC lines) or cytosol (CYS lines), we explored the hypothesis that cysteine proteases regulate photosynthesis. The CYS and PC l...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Oxford University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8256631/ https://www.ncbi.nlm.nih.gov/pubmed/33686435 http://dx.doi.org/10.1093/jxb/erab101 |
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author | Alomrani, Sarah Kunert, Karl J Foyer, Christine H |
author_facet | Alomrani, Sarah Kunert, Karl J Foyer, Christine H |
author_sort | Alomrani, Sarah |
collection | PubMed |
description | Chloroplasts are considered to be devoid of cysteine proteases. Using transgenic Arabidopsis lines expressing the rice cystatin, oryzacystatin I (OC-I), in the chloroplasts (PC lines) or cytosol (CYS lines), we explored the hypothesis that cysteine proteases regulate photosynthesis. The CYS and PC lines flowered later than the wild type (WT) and accumulated more biomass after flowering. In contrast to the PC rosettes, which accumulated more leaf chlorophyll and carotenoid pigments than the WT, the CYS lines had lower amounts of leaf pigments. High-light-dependent decreases in photosynthetic carbon assimilation and the abundance of the Rubisco large subunit protein, the D1 protein, and the phosphorylated form of D1 proteins were attenuated in the CYS lines and reversed in the PC lines relative to the WT. However, the transgenic lines had higher amounts of LHC, rbcs, pasbA, and pasbD transcripts than the WT, and also showed modified chloroplast to nucleus signalling. We conclude that cysteine proteases accelerate the reconfiguration of the chloroplast proteome after flowering and in response to high-light stress. Inhibition of cysteine proteases, such as AtCEP1, slows chloroplast protein degradation and stimulates photosynthetic gene expression and chloroplast to nucleus signalling, enhancing stress tolerance traits. |
format | Online Article Text |
id | pubmed-8256631 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-82566312021-07-06 Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress Alomrani, Sarah Kunert, Karl J Foyer, Christine H J Exp Bot Research Papers Chloroplasts are considered to be devoid of cysteine proteases. Using transgenic Arabidopsis lines expressing the rice cystatin, oryzacystatin I (OC-I), in the chloroplasts (PC lines) or cytosol (CYS lines), we explored the hypothesis that cysteine proteases regulate photosynthesis. The CYS and PC lines flowered later than the wild type (WT) and accumulated more biomass after flowering. In contrast to the PC rosettes, which accumulated more leaf chlorophyll and carotenoid pigments than the WT, the CYS lines had lower amounts of leaf pigments. High-light-dependent decreases in photosynthetic carbon assimilation and the abundance of the Rubisco large subunit protein, the D1 protein, and the phosphorylated form of D1 proteins were attenuated in the CYS lines and reversed in the PC lines relative to the WT. However, the transgenic lines had higher amounts of LHC, rbcs, pasbA, and pasbD transcripts than the WT, and also showed modified chloroplast to nucleus signalling. We conclude that cysteine proteases accelerate the reconfiguration of the chloroplast proteome after flowering and in response to high-light stress. Inhibition of cysteine proteases, such as AtCEP1, slows chloroplast protein degradation and stimulates photosynthetic gene expression and chloroplast to nucleus signalling, enhancing stress tolerance traits. Oxford University Press 2021-03-04 /pmc/articles/PMC8256631/ /pubmed/33686435 http://dx.doi.org/10.1093/jxb/erab101 Text en © The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissions@oup.com https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Papers Alomrani, Sarah Kunert, Karl J Foyer, Christine H Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
title | Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
title_full | Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
title_fullStr | Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
title_full_unstemmed | Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
title_short | Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
title_sort | papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8256631/ https://www.ncbi.nlm.nih.gov/pubmed/33686435 http://dx.doi.org/10.1093/jxb/erab101 |
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