Control of plastidial metabolism by the Clp protease complex

Plant metabolism is strongly dependent on plastids. Besides hosting the photosynthetic machinery, these endosymbiotic organelles synthesize starch, fatty acids, amino acids, nucleotides, tetrapyrroles, and isoprenoids. Virtually all enzymes involved in plastid-localized metabolic pathways are encode...

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Autores: Rodriguez-Concepcion, Manuel, D’Andrea, Lucio, Pulido, Pablo
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/206657
Acceso en línea:http://hdl.handle.net/10261/206657
Access Level:acceso abierto
Palabra clave:Carotenoids
Chaperone
Chlorophyll
Chloroplast
Clp protease
Chromoplasts
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spelling Control of plastidial metabolism by the Clp protease complexRodriguez-Concepcion, ManuelD’Andrea, LucioPulido, PabloCarotenoidsChaperoneChlorophyllChloroplastClp proteaseChromoplastsPlant metabolism is strongly dependent on plastids. Besides hosting the photosynthetic machinery, these endosymbiotic organelles synthesize starch, fatty acids, amino acids, nucleotides, tetrapyrroles, and isoprenoids. Virtually all enzymes involved in plastid-localized metabolic pathways are encoded by the nuclear genome and imported into plastids. Once there, protein quality control systems ensure proper folding of the mature forms and remove irreversibly damaged proteins. The Clp protease is the main machinery for protein degradation in the plastid stroma. Recent work has unveiled an increasing number of client proteins of this proteolytic complex in plants. Notably, a substantial proportion of these substrates are required for normal chloroplast metabolism, including enzymes involved in the production of essential tetrapyrroles and isoprenoids such as chlorophylls and carotenoids. The Clp protease complex acts in coordination with nuclear-encoded plastidial chaperones for the control of both enzyme levels and proper folding (i.e. activity). This communication involves a retrograde signaling pathway, similarly to the unfolded protein response previously characterized in mitochondria and endoplasmic reticulum. Coordinated Clp protease and chaperone activities appear to further influence other plastid processes, such as the differentiation of chloroplasts into carotenoid-accumulating chromoplasts during fruit ripening.Work in our lab is funded by grants BIO2015-71703-REDT, BIO2017-90877-REDT and BIO2017-84041-P from the Spanish Ministry of Economy and Competitiveness (MINECO), 2017SGR-710 from Generalitat de Catalunya, and CA15136 (COST action EuroCaroten) from the European Commission H2020 program. We also thank the financial support of the MINECO Severo Ochoa Programme for Centres of Excellence in R&D 2016–2019 (SEV-2015-0533) and the Generalitat de Catalunya CERCA Programme to CRAG.Peer reviewedOxford University PressMinisterio de Ciencia, Innovación y Universidades (España)Ministerio de Economía y Competitividad (España)Generalitat de CatalunyaEuropean CommissionAgencia Estatal de Investigación (España)Rodríguez-Concepción, Manuel [0000-0002-1280-2305]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202020202019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/206657reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2015-71703-REDTinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/BIO2017-90877-REDTBIO2017-90877-REDT/AEI/10.13039/501100011033info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/BIO2017-84041-PBIO2017-84041-P/AEI/10.13039/501100011033https://doi.org/10.1093/jxb/ery441Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2066572026-05-22T06:33:51Z
dc.title.none.fl_str_mv Control of plastidial metabolism by the Clp protease complex
title Control of plastidial metabolism by the Clp protease complex
spellingShingle Control of plastidial metabolism by the Clp protease complex
Rodriguez-Concepcion, Manuel
Carotenoids
Chaperone
Chlorophyll
Chloroplast
Clp protease
Chromoplasts
title_short Control of plastidial metabolism by the Clp protease complex
title_full Control of plastidial metabolism by the Clp protease complex
title_fullStr Control of plastidial metabolism by the Clp protease complex
title_full_unstemmed Control of plastidial metabolism by the Clp protease complex
title_sort Control of plastidial metabolism by the Clp protease complex
dc.creator.none.fl_str_mv Rodriguez-Concepcion, Manuel
D’Andrea, Lucio
Pulido, Pablo
author Rodriguez-Concepcion, Manuel
author_facet Rodriguez-Concepcion, Manuel
D’Andrea, Lucio
Pulido, Pablo
author_role author
author2 D’Andrea, Lucio
Pulido, Pablo
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Ministerio de Economía y Competitividad (España)
Generalitat de Catalunya
European Commission
Agencia Estatal de Investigación (España)
Rodríguez-Concepción, Manuel [0000-0002-1280-2305]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Carotenoids
Chaperone
Chlorophyll
Chloroplast
Clp protease
Chromoplasts
topic Carotenoids
Chaperone
Chlorophyll
Chloroplast
Clp protease
Chromoplasts
description Plant metabolism is strongly dependent on plastids. Besides hosting the photosynthetic machinery, these endosymbiotic organelles synthesize starch, fatty acids, amino acids, nucleotides, tetrapyrroles, and isoprenoids. Virtually all enzymes involved in plastid-localized metabolic pathways are encoded by the nuclear genome and imported into plastids. Once there, protein quality control systems ensure proper folding of the mature forms and remove irreversibly damaged proteins. The Clp protease is the main machinery for protein degradation in the plastid stroma. Recent work has unveiled an increasing number of client proteins of this proteolytic complex in plants. Notably, a substantial proportion of these substrates are required for normal chloroplast metabolism, including enzymes involved in the production of essential tetrapyrroles and isoprenoids such as chlorophylls and carotenoids. The Clp protease complex acts in coordination with nuclear-encoded plastidial chaperones for the control of both enzyme levels and proper folding (i.e. activity). This communication involves a retrograde signaling pathway, similarly to the unfolded protein response previously characterized in mitochondria and endoplasmic reticulum. Coordinated Clp protease and chaperone activities appear to further influence other plastid processes, such as the differentiation of chloroplasts into carotenoid-accumulating chromoplasts during fruit ripening.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/206657
url http://hdl.handle.net/10261/206657
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2015-71703-REDT
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/BIO2017-90877-REDT
BIO2017-90877-REDT/AEI/10.13039/501100011033
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/BIO2017-84041-P
BIO2017-84041-P/AEI/10.13039/501100011033
https://doi.org/10.1093/jxb/ery441
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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