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Possible compensatory role among chloroplast proteases under excess-light stress condition

The reaction center protein D1 of photosystem II (PSII), known as a primary target of photodamage, is repaired efficiently by the PSII repair cycle, to cope with constant photooxidative damage. Recent studies of Arabidopsis show that the endo-type Deg protease and the exo-type FtsH proteases coopera...

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Autores principales: Kato, Yusuke, Sakamoto, Wataru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676490/
https://www.ncbi.nlm.nih.gov/pubmed/23299325
http://dx.doi.org/10.4161/psb.23198
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author Kato, Yusuke
Sakamoto, Wataru
author_facet Kato, Yusuke
Sakamoto, Wataru
author_sort Kato, Yusuke
collection PubMed
description The reaction center protein D1 of photosystem II (PSII), known as a primary target of photodamage, is repaired efficiently by the PSII repair cycle, to cope with constant photooxidative damage. Recent studies of Arabidopsis show that the endo-type Deg protease and the exo-type FtsH proteases cooperatively degrade D1 in the PSII repair in vivo. It is particularly interesting that we observed upregulation of Clp and SppA proteases when FtsH was limited in the mutant lacking FtsH2. To examine how the complementary functions of chloroplastic proteases are commonly regulated, we undertook a high-light stress on wild-type Arabidopsis leaves. The result that wild type leaves also showed increased levels of these proteases upon exposure to excessively strong illumination not only revealed the importance of FtsH and Deg in the PSII repair, but also implied cooperation among chloroplastic proteases under chronic stress conditions.
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spelling pubmed-36764902013-06-14 Possible compensatory role among chloroplast proteases under excess-light stress condition Kato, Yusuke Sakamoto, Wataru Plant Signal Behav Short Communication The reaction center protein D1 of photosystem II (PSII), known as a primary target of photodamage, is repaired efficiently by the PSII repair cycle, to cope with constant photooxidative damage. Recent studies of Arabidopsis show that the endo-type Deg protease and the exo-type FtsH proteases cooperatively degrade D1 in the PSII repair in vivo. It is particularly interesting that we observed upregulation of Clp and SppA proteases when FtsH was limited in the mutant lacking FtsH2. To examine how the complementary functions of chloroplastic proteases are commonly regulated, we undertook a high-light stress on wild-type Arabidopsis leaves. The result that wild type leaves also showed increased levels of these proteases upon exposure to excessively strong illumination not only revealed the importance of FtsH and Deg in the PSII repair, but also implied cooperation among chloroplastic proteases under chronic stress conditions. Landes Bioscience 2013-03-01 2013-01-08 /pmc/articles/PMC3676490/ /pubmed/23299325 http://dx.doi.org/10.4161/psb.23198 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Short Communication
Kato, Yusuke
Sakamoto, Wataru
Possible compensatory role among chloroplast proteases under excess-light stress condition
title Possible compensatory role among chloroplast proteases under excess-light stress condition
title_full Possible compensatory role among chloroplast proteases under excess-light stress condition
title_fullStr Possible compensatory role among chloroplast proteases under excess-light stress condition
title_full_unstemmed Possible compensatory role among chloroplast proteases under excess-light stress condition
title_short Possible compensatory role among chloroplast proteases under excess-light stress condition
title_sort possible compensatory role among chloroplast proteases under excess-light stress condition
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676490/
https://www.ncbi.nlm.nih.gov/pubmed/23299325
http://dx.doi.org/10.4161/psb.23198
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