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Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?

Autophagy is essential for protein degradation, nutrient recycling, and nitrogen remobilization. Autophagy is induced during leaf ageing and in response to nitrogen starvation, and is known to play a fundamental role in nutrient recycling for remobilization and seed filling. Accordingly, ageing leav...

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Autores principales: Havé, Marien, Balliau, Thierry, Cottyn-Boitte, Betty, Dérond, Emeline, Cueff, Gwendal, Soulay, Fabienne, Lornac, Aurélia, Reichman, Pavel, Dissmeyer, Nico, Avice, Jean-Christophe, Gallois, Patrick, Rajjou, Loïc, Zivy, Michel, Masclaux-Daubresse, Céline
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6037082/
https://www.ncbi.nlm.nih.gov/pubmed/29281085
http://dx.doi.org/10.1093/jxb/erx482
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author Havé, Marien
Balliau, Thierry
Cottyn-Boitte, Betty
Dérond, Emeline
Cueff, Gwendal
Soulay, Fabienne
Lornac, Aurélia
Reichman, Pavel
Dissmeyer, Nico
Avice, Jean-Christophe
Gallois, Patrick
Rajjou, Loïc
Zivy, Michel
Masclaux-Daubresse, Céline
author_facet Havé, Marien
Balliau, Thierry
Cottyn-Boitte, Betty
Dérond, Emeline
Cueff, Gwendal
Soulay, Fabienne
Lornac, Aurélia
Reichman, Pavel
Dissmeyer, Nico
Avice, Jean-Christophe
Gallois, Patrick
Rajjou, Loïc
Zivy, Michel
Masclaux-Daubresse, Céline
author_sort Havé, Marien
collection PubMed
description Autophagy is essential for protein degradation, nutrient recycling, and nitrogen remobilization. Autophagy is induced during leaf ageing and in response to nitrogen starvation, and is known to play a fundamental role in nutrient recycling for remobilization and seed filling. Accordingly, ageing leaves of Arabidopsis autophagy mutants (atg) have been shown to over-accumulate proteins and peptides, possibly because of a reduced protein degradation capacity. Surprisingly, atg leaves also displayed higher protease activities. The work reported here aimed at identifying the nature of the proteases and protease activities that accumulated differentially (higher or lower) in the atg mutants. Protease identification was performed using shotgun LC-MS/MS proteome analyses and activity-based protein profiling (ABPP). The results showed that the chloroplast FTSH (FILAMENTATION TEMPERATURE SENSITIVE H) and DEG (DEGRADATION OF PERIPLASMIC PROTEINS) proteases and several extracellular serine proteases [subtilases (SBTs) and serine carboxypeptidase-like (SCPL) proteases] were less abundant in atg5 mutants. By contrast, proteasome-related proteins and cytosolic or vacuole cysteine proteases were more abundant in atg5 mutants. Rubisco degradation assays and ABPP showed that the activities of proteasome and papain-like cysteine protease were increased in atg5 mutants. Whether these proteases play a back-up role in nutrient recycling and remobilization in atg mutants or act to promote cell death is discussed in relation to their accumulation patterns in the atg5 mutant compared with the salicylic acid-depleted atg5/sid2 double-mutant, and in low nitrate compared with high nitrate conditions. Several of the proteins identified are indeed known as senescence- and stress-related proteases or as spontaneous cell-death triggering factors.
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spelling pubmed-60370822018-07-12 Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect? Havé, Marien Balliau, Thierry Cottyn-Boitte, Betty Dérond, Emeline Cueff, Gwendal Soulay, Fabienne Lornac, Aurélia Reichman, Pavel Dissmeyer, Nico Avice, Jean-Christophe Gallois, Patrick Rajjou, Loïc Zivy, Michel Masclaux-Daubresse, Céline J Exp Bot Research Papers Autophagy is essential for protein degradation, nutrient recycling, and nitrogen remobilization. Autophagy is induced during leaf ageing and in response to nitrogen starvation, and is known to play a fundamental role in nutrient recycling for remobilization and seed filling. Accordingly, ageing leaves of Arabidopsis autophagy mutants (atg) have been shown to over-accumulate proteins and peptides, possibly because of a reduced protein degradation capacity. Surprisingly, atg leaves also displayed higher protease activities. The work reported here aimed at identifying the nature of the proteases and protease activities that accumulated differentially (higher or lower) in the atg mutants. Protease identification was performed using shotgun LC-MS/MS proteome analyses and activity-based protein profiling (ABPP). The results showed that the chloroplast FTSH (FILAMENTATION TEMPERATURE SENSITIVE H) and DEG (DEGRADATION OF PERIPLASMIC PROTEINS) proteases and several extracellular serine proteases [subtilases (SBTs) and serine carboxypeptidase-like (SCPL) proteases] were less abundant in atg5 mutants. By contrast, proteasome-related proteins and cytosolic or vacuole cysteine proteases were more abundant in atg5 mutants. Rubisco degradation assays and ABPP showed that the activities of proteasome and papain-like cysteine protease were increased in atg5 mutants. Whether these proteases play a back-up role in nutrient recycling and remobilization in atg mutants or act to promote cell death is discussed in relation to their accumulation patterns in the atg5 mutant compared with the salicylic acid-depleted atg5/sid2 double-mutant, and in low nitrate compared with high nitrate conditions. Several of the proteins identified are indeed known as senescence- and stress-related proteases or as spontaneous cell-death triggering factors. Oxford University Press 2018-03-05 2018-01-27 /pmc/articles/PMC6037082/ /pubmed/29281085 http://dx.doi.org/10.1093/jxb/erx482 Text en © The Author(s) 2018. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://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/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Papers
Havé, Marien
Balliau, Thierry
Cottyn-Boitte, Betty
Dérond, Emeline
Cueff, Gwendal
Soulay, Fabienne
Lornac, Aurélia
Reichman, Pavel
Dissmeyer, Nico
Avice, Jean-Christophe
Gallois, Patrick
Rajjou, Loïc
Zivy, Michel
Masclaux-Daubresse, Céline
Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
title Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
title_full Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
title_fullStr Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
title_full_unstemmed Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
title_short Increases in activity of proteasome and papain-like cysteine protease in Arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
title_sort increases in activity of proteasome and papain-like cysteine protease in arabidopsis autophagy mutants: back-up compensatory effect or cell-death promoting effect?
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6037082/
https://www.ncbi.nlm.nih.gov/pubmed/29281085
http://dx.doi.org/10.1093/jxb/erx482
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