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Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition

The EGY3 is a pseudoprotease, located in the thylakoid membrane, that shares homology with the family of site-2-proteases (S2P). Although S2P proteases are present in the cells of all living organisms, the EGY3 was found only in plant cells. The sequence of the pseudoprotease is highly conserved in...

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Autores principales: Adamiec, Małgorzata, Dobrogojski, Jędrzej, Wojtyla, Łukasz, Luciński, Robert
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9355673/
https://www.ncbi.nlm.nih.gov/pubmed/35937369
http://dx.doi.org/10.3389/fpls.2022.965143
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author Adamiec, Małgorzata
Dobrogojski, Jędrzej
Wojtyla, Łukasz
Luciński, Robert
author_facet Adamiec, Małgorzata
Dobrogojski, Jędrzej
Wojtyla, Łukasz
Luciński, Robert
author_sort Adamiec, Małgorzata
collection PubMed
description The EGY3 is a pseudoprotease, located in the thylakoid membrane, that shares homology with the family of site-2-proteases (S2P). Although S2P proteases are present in the cells of all living organisms, the EGY3 was found only in plant cells. The sequence of the pseudoprotease is highly conserved in the plant kingdom; however, little is known about its physiological importance. Results obtained with real-time PCR indicated that the expression of the EGY3 gene is dramatically induced during the first few hours of exposure to high light and high-temperature stress. The observed increase in transcript abundance correlates with protein accumulation level, which indicates that EGY3 participates in response to both high-temperature and high light stresses. The lack of the pseudoprotease leads, in both stresses, to lower concentrations of hydrogen peroxide. However, the decrease of chloroplast copper/zinc superoxide dismutase 2 level was observed only during the high light stress. In both analyzed stressful conditions, proteins related to RubisCO folding, glycine metabolism, and photosystem I were identified as differently accumulating in egy3 mutant lines and WT plants; however, the functional status of PSII during analyzed stressful conditions remains very similar. Our results lead to a conclusion that EGY3 pseudoprotease participates in response to high light and high-temperature stress; however, its role is associated rather with photosystem I and light-independent reactions of photosynthesis.
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spelling pubmed-93556732022-08-06 Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition Adamiec, Małgorzata Dobrogojski, Jędrzej Wojtyla, Łukasz Luciński, Robert Front Plant Sci Plant Science The EGY3 is a pseudoprotease, located in the thylakoid membrane, that shares homology with the family of site-2-proteases (S2P). Although S2P proteases are present in the cells of all living organisms, the EGY3 was found only in plant cells. The sequence of the pseudoprotease is highly conserved in the plant kingdom; however, little is known about its physiological importance. Results obtained with real-time PCR indicated that the expression of the EGY3 gene is dramatically induced during the first few hours of exposure to high light and high-temperature stress. The observed increase in transcript abundance correlates with protein accumulation level, which indicates that EGY3 participates in response to both high-temperature and high light stresses. The lack of the pseudoprotease leads, in both stresses, to lower concentrations of hydrogen peroxide. However, the decrease of chloroplast copper/zinc superoxide dismutase 2 level was observed only during the high light stress. In both analyzed stressful conditions, proteins related to RubisCO folding, glycine metabolism, and photosystem I were identified as differently accumulating in egy3 mutant lines and WT plants; however, the functional status of PSII during analyzed stressful conditions remains very similar. Our results lead to a conclusion that EGY3 pseudoprotease participates in response to high light and high-temperature stress; however, its role is associated rather with photosystem I and light-independent reactions of photosynthesis. Frontiers Media S.A. 2022-07-22 /pmc/articles/PMC9355673/ /pubmed/35937369 http://dx.doi.org/10.3389/fpls.2022.965143 Text en Copyright © 2022 Adamiec, Dobrogojski, Wojtyla and Luciński. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Adamiec, Małgorzata
Dobrogojski, Jędrzej
Wojtyla, Łukasz
Luciński, Robert
Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
title Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
title_full Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
title_fullStr Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
title_full_unstemmed Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
title_short Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
title_sort stress-related expression of the chloroplast egy3 pseudoprotease and its possible impact on chloroplasts’ proteome composition
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9355673/
https://www.ncbi.nlm.nih.gov/pubmed/35937369
http://dx.doi.org/10.3389/fpls.2022.965143
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