Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions

Fibrillins (FBNs) are plastidial proteins found in photosynthetic organisms from cyanobacteria to higher plants. The function of most FBNs remains unknown. Here, we focused on members of the FBN subgroup comprising FBN1a, FBN1b, and FBN2. We show that these three polypeptides interact between each o...

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Autores: Torres-Romero, Diego, Gómez-Zambrano, Ángeles, Serrato, Antonio Jesús, Sahrawy, Mariam, Mérida, Ángel
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2022
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/275811
Acesso em linha:http://hdl.handle.net/10261/275811
Access Level:Acceso aberto
Palavra-chave:Abiotic stress
Arabidopsis
Fibrillin
Jasmonate
Photosystem II
Plastoglobule
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spelling Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactionsTorres-Romero, DiegoGómez-Zambrano, ÁngelesSerrato, Antonio JesúsSahrawy, MariamMérida, ÁngelAbiotic stressArabidopsisFibrillinJasmonatePhotosystem IIPlastoglobuleFibrillins (FBNs) are plastidial proteins found in photosynthetic organisms from cyanobacteria to higher plants. The function of most FBNs remains unknown. Here, we focused on members of the FBN subgroup comprising FBN1a, FBN1b, and FBN2. We show that these three polypeptides interact between each other, potentially forming a network around the plastoglobule surface. Both FBN2 and FBN1s interact with allene oxide synthase, and the elimination of any of these FBNs results in a delay in jasmonate-mediated anthocyanin accumulation in response to a combination of moderate high light and low temperature. Mutations in the genes encoding FBN1s or FBN2 also affect the protection of PSII under the combination of these stresses. Fully developed leaves of these mutants have lower maximum quantum efficiency of PSII (Fv/Fm) and higher oxidative stress than wild-type plants. These effects are additive, and the fbn1a-1b-2 triple mutant shows a stronger decrease in Fv/Fm and a greater increase in oxidative stress than fbn1a-1b or fbn2 mutants. Co-immunoprecipitation analysis indicated that FBN2 also interacts with other proteins involved in different metabolic processes. We propose that these fibrillins facilitate accurate positioning of different proteins involved in distinct metabolic processes, and that their elimination leads to dysfunction of those proteins.DTR was the recipient of a “Formación de Personal Investigador” (FPI) fellowship from the Spanish Ministry of Economy and Competitiveness (MINECO). This work was funded by grants BIO2015-65272-C2-1-P and BIO2015-65272-C2-2-P from the MINECO and the European Fund for Regional Development, and grants PGC2018-096851-B-C21 and PGC2018-096851-B-C22 from the Spanish Ministry of Science and Innovation (MICINN) and the European Fund for Regional Development.Oxford University PressMinisterio de Economía y Competitividad (España)European CommissionMinisterio de Ciencia e Innovación (España)Consejo 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/10261/275811reponame: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#info:eu-repo/grantAgreement/MINECO//BIO2015-65272-C2-1-Pinfo:eu-repo/grantAgreement/MINECO//BIO2015-65272-C2-2-Pinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-096851-B-C21info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-096851-B-C22http://dx.doi.org/10.1093/jxb/erab452Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2758112026-05-22T06:33:51Z
dc.title.none.fl_str_mv Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
title Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
spellingShingle Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
Torres-Romero, Diego
Abiotic stress
Arabidopsis
Fibrillin
Jasmonate
Photosystem II
Plastoglobule
title_short Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
title_full Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
title_fullStr Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
title_full_unstemmed Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
title_sort Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions
dc.creator.none.fl_str_mv Torres-Romero, Diego
Gómez-Zambrano, Ángeles
Serrato, Antonio Jesús
Sahrawy, Mariam
Mérida, Ángel
author Torres-Romero, Diego
author_facet Torres-Romero, Diego
Gómez-Zambrano, Ángeles
Serrato, Antonio Jesús
Sahrawy, Mariam
Mérida, Ángel
author_role author
author2 Gómez-Zambrano, Ángeles
Serrato, Antonio Jesús
Sahrawy, Mariam
Mérida, Ángel
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
European Commission
Ministerio de Ciencia e Innovación (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Abiotic stress
Arabidopsis
Fibrillin
Jasmonate
Photosystem II
Plastoglobule
topic Abiotic stress
Arabidopsis
Fibrillin
Jasmonate
Photosystem II
Plastoglobule
description Fibrillins (FBNs) are plastidial proteins found in photosynthetic organisms from cyanobacteria to higher plants. The function of most FBNs remains unknown. Here, we focused on members of the FBN subgroup comprising FBN1a, FBN1b, and FBN2. We show that these three polypeptides interact between each other, potentially forming a network around the plastoglobule surface. Both FBN2 and FBN1s interact with allene oxide synthase, and the elimination of any of these FBNs results in a delay in jasmonate-mediated anthocyanin accumulation in response to a combination of moderate high light and low temperature. Mutations in the genes encoding FBN1s or FBN2 also affect the protection of PSII under the combination of these stresses. Fully developed leaves of these mutants have lower maximum quantum efficiency of PSII (Fv/Fm) and higher oxidative stress than wild-type plants. These effects are additive, and the fbn1a-1b-2 triple mutant shows a stronger decrease in Fv/Fm and a greater increase in oxidative stress than fbn1a-1b or fbn2 mutants. Co-immunoprecipitation analysis indicated that FBN2 also interacts with other proteins involved in different metabolic processes. We propose that these fibrillins facilitate accurate positioning of different proteins involved in distinct metabolic processes, and that their elimination leads to dysfunction of those proteins.
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/10261/275811
url http://hdl.handle.net/10261/275811
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
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info:eu-repo/grantAgreement/MINECO//BIO2015-65272-C2-1-P
info:eu-repo/grantAgreement/MINECO//BIO2015-65272-C2-2-P
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-096851-B-C21
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-096851-B-C22
http://dx.doi.org/10.1093/jxb/erab452

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
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