Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis

Peroxisomes are ubiquitous organelles from eukaryotic cells characterized by an active nitro-oxidative metabolism. They have a relevant metabolic plasticity depending on the organism, tissue, developmental stage, or physiological/stress/environmental conditions. Our knowledge of peroxisomal metaboli...

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Autores: González-Gordo, Salvador, Palma Martínez, José Manuel, Corpas, Francisco J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/276254
Acceso en línea:http://hdl.handle.net/10261/276254
Access Level:acceso abierto
Palabra clave:iTRAQ
Phenylpropanoids
Pepper fruit
Ripening
Jasmonic acid
Peroxisomes
Proteome
Sulfite oxidase
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spelling Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysisGonzález-Gordo, SalvadorPalma Martínez, José ManuelCorpas, Francisco J.iTRAQPhenylpropanoidsPepper fruitRipeningJasmonic acidPeroxisomesProteomeSulfite oxidasePeroxisomes are ubiquitous organelles from eukaryotic cells characterized by an active nitro-oxidative metabolism. They have a relevant metabolic plasticity depending on the organism, tissue, developmental stage, or physiological/stress/environmental conditions. Our knowledge of peroxisomal metabolism from fruits is very limited but its proteome is even less known. Using sweet pepper (Capsicum annuum L.) fruits at two ripening stages (immature green and ripe red), it was analyzed the proteomic peroxisomal composition by quantitative isobaric tags for relative and absolute quantitation (iTRAQ)-based protein profiling. For this aim, it was accomplished a comparative analysis of the pepper fruit whole proteome obtained by iTRAQ versus the identified peroxisomal protein profile from Arabidopsis thaliana. This allowed identifying 57 peroxisomal proteins. Among these proteins, 49 were located in the peroxisomal matrix, 36 proteins had a peroxisomal targeting signal type 1 (PTS1), 8 had a PTS type 2, 5 lacked this type of peptide signal, and 8 proteins were associated with the membrane of this organelle. Furthermore, 34 proteins showed significant differences during the ripening of the fruits, 19 being overexpressed and 15 repressed. Based on previous biochemical studies using purified peroxisomes from pepper fruits, it could be said that some of the identified peroxisomal proteins were corroborated as part of the pepper fruit antioxidant metabolism (catalase, superoxide dismutase, ascorbate peroxidase, monodehydroascorbate reductase, dehydroascorbate reductaseglutathione reductase, 6-phosphogluconate dehydrogenase and NADP-isocitrate dehydrogenase), the β-oxidation pathway (acyl-coenzyme A oxidase, 3-hydroxyacyl-CoA dehydrogenase, enoyl-CoA hydratase), while other identified proteins could be considered “new” or “unexpected” in fruit peroxisomes like urate oxidase (UO), sulfite oxidase (SO), 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase (METE1), 12-oxophytodienoate reductase 3 (OPR3) or 4-coumarate-CoA ligase (4CL), which participate in different metabolic pathways such as purine, sulfur, L-methionine, jasmonic acid (JA) or phenylpropanoid metabolisms. In summary, the present data provide new insights into the complex metabolic machinery of peroxisomes in fruit and open new windows of research into the peroxisomal functions during fruit ripening.Our research is supported by a European Regional Development Fund-cofinanced grant from the Ministry of Economy and Competitiveness (PID2019-103924GB-I00), and the Plan Andaluz de Investigación, Desarrollo e Innovación (PAIDI 2020) (P18-FR-1359), Spain.Frontiers MediaEuropean CommissionMinisterio de Economía y Competitividad (España)Junta de AndalucíaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2022202220222022info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/276254reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103924GB-I00http://dx.doi.org/10.3389/fpls.2022.893376Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2762542026-05-22T06:33:51Z
dc.title.none.fl_str_mv Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
title Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
spellingShingle Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
González-Gordo, Salvador
iTRAQ
Phenylpropanoids
Pepper fruit
Ripening
Jasmonic acid
Peroxisomes
Proteome
Sulfite oxidase
title_short Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
title_full Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
title_fullStr Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
title_full_unstemmed Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
title_sort Peroxisomal proteome mining of sweet pepper (Capsicum annuum L.) fruit ripening through whole isobaric tags for relative and absolute quantitation analysis
dc.creator.none.fl_str_mv González-Gordo, Salvador
Palma Martínez, José Manuel
Corpas, Francisco J.
author González-Gordo, Salvador
author_facet González-Gordo, Salvador
Palma Martínez, José Manuel
Corpas, Francisco J.
author_role author
author2 Palma Martínez, José Manuel
Corpas, Francisco J.
author2_role author
author
dc.contributor.none.fl_str_mv European Commission
Ministerio de Economía y Competitividad (España)
Junta de Andalucía
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv iTRAQ
Phenylpropanoids
Pepper fruit
Ripening
Jasmonic acid
Peroxisomes
Proteome
Sulfite oxidase
topic iTRAQ
Phenylpropanoids
Pepper fruit
Ripening
Jasmonic acid
Peroxisomes
Proteome
Sulfite oxidase
description Peroxisomes are ubiquitous organelles from eukaryotic cells characterized by an active nitro-oxidative metabolism. They have a relevant metabolic plasticity depending on the organism, tissue, developmental stage, or physiological/stress/environmental conditions. Our knowledge of peroxisomal metabolism from fruits is very limited but its proteome is even less known. Using sweet pepper (Capsicum annuum L.) fruits at two ripening stages (immature green and ripe red), it was analyzed the proteomic peroxisomal composition by quantitative isobaric tags for relative and absolute quantitation (iTRAQ)-based protein profiling. For this aim, it was accomplished a comparative analysis of the pepper fruit whole proteome obtained by iTRAQ versus the identified peroxisomal protein profile from Arabidopsis thaliana. This allowed identifying 57 peroxisomal proteins. Among these proteins, 49 were located in the peroxisomal matrix, 36 proteins had a peroxisomal targeting signal type 1 (PTS1), 8 had a PTS type 2, 5 lacked this type of peptide signal, and 8 proteins were associated with the membrane of this organelle. Furthermore, 34 proteins showed significant differences during the ripening of the fruits, 19 being overexpressed and 15 repressed. Based on previous biochemical studies using purified peroxisomes from pepper fruits, it could be said that some of the identified peroxisomal proteins were corroborated as part of the pepper fruit antioxidant metabolism (catalase, superoxide dismutase, ascorbate peroxidase, monodehydroascorbate reductase, dehydroascorbate reductaseglutathione reductase, 6-phosphogluconate dehydrogenase and NADP-isocitrate dehydrogenase), the β-oxidation pathway (acyl-coenzyme A oxidase, 3-hydroxyacyl-CoA dehydrogenase, enoyl-CoA hydratase), while other identified proteins could be considered “new” or “unexpected” in fruit peroxisomes like urate oxidase (UO), sulfite oxidase (SO), 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase (METE1), 12-oxophytodienoate reductase 3 (OPR3) or 4-coumarate-CoA ligase (4CL), which participate in different metabolic pathways such as purine, sulfur, L-methionine, jasmonic acid (JA) or phenylpropanoid metabolisms. In summary, the present data provide new insights into the complex metabolic machinery of peroxisomes in fruit and open new windows of research into the peroxisomal functions during fruit ripening.
publishDate 2022
dc.date.none.fl_str_mv 2022
2022
2022
2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/276254
url http://hdl.handle.net/10261/276254
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103924GB-I00
http://dx.doi.org/10.3389/fpls.2022.893376
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
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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