CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis

Flowering time is a key process in plant development. Photoperiodic signals play a crucial role in the floral transition in Arabidopsis thaliana, and the protein CONSTANS (CO) has a central regulatory function that is tightly regulated at the transcriptional and post-translational levels. The stabil...

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Autores: Serrano-Bueno, Gloria, Said, Fátima E., Reyes, Pedro de los, Lucas-Reina, Eva, Ortíz-Marchena, M. Isabel, Romero, José M., Valverde, Federico
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/216533
Acceso en línea:http://hdl.handle.net/10261/216533
Access Level:acceso abierto
Palabra clave:Floral transition
Photoperiodic flowering
CONSTANS
Posttranslational modification
Protein stability
FKBP12
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spelling CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in ArabidopsisSerrano-Bueno, GloriaSaid, Fátima E.Reyes, Pedro de losLucas-Reina, EvaOrtíz-Marchena, M. IsabelRomero, José M.Valverde, FedericoFloral transitionPhotoperiodic floweringCONSTANSPosttranslational modificationProtein stabilityFKBP12Flowering time is a key process in plant development. Photoperiodic signals play a crucial role in the floral transition in Arabidopsis thaliana, and the protein CONSTANS (CO) has a central regulatory function that is tightly regulated at the transcriptional and post-translational levels. The stability of CO protein depends on a light-driven proteasome process that optimizes its accumulation in the evening to promote the production of the florigen FLOWERING LOCUS T (FT) and induce seasonal flowering. To further investigate the post-translational regulation of CO protein we have dissected its interactome network employing in vivo and in vitro assays and molecular genetics approaches. The immunophilin FKBP12 has been identified in Arabidopsis as a CO interactor that regulates its accumulation and activity. FKBP12 and CO interact through the CCT domain, affecting the stability and function of CO. fkbp12 insertion mutants show a delay in flowering time, while FKBP12 overexpression accelerates flowering, and these phenotypes can be directly related to a change in accumulation of FT protein. The interaction is conserved between the Chlamydomonas algal orthologs CrCO–CrFKBP12, revealing an ancient regulatory step in photoperiod regulation of plant development.Blackwell PublishingConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2020202020202020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/216533reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1111/tpj.14590Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2165332026-05-22T06:33:51Z
dc.title.none.fl_str_mv CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
title CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
spellingShingle CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
Serrano-Bueno, Gloria
Floral transition
Photoperiodic flowering
CONSTANS
Posttranslational modification
Protein stability
FKBP12
title_short CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
title_full CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
title_fullStr CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
title_full_unstemmed CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
title_sort CONSTANS–FKBP12 interaction contributes to modulation of photoperiodic flowering in Arabidopsis
dc.creator.none.fl_str_mv Serrano-Bueno, Gloria
Said, Fátima E.
Reyes, Pedro de los
Lucas-Reina, Eva
Ortíz-Marchena, M. Isabel
Romero, José M.
Valverde, Federico
author Serrano-Bueno, Gloria
author_facet Serrano-Bueno, Gloria
Said, Fátima E.
Reyes, Pedro de los
Lucas-Reina, Eva
Ortíz-Marchena, M. Isabel
Romero, José M.
Valverde, Federico
author_role author
author2 Said, Fátima E.
Reyes, Pedro de los
Lucas-Reina, Eva
Ortíz-Marchena, M. Isabel
Romero, José M.
Valverde, Federico
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Floral transition
Photoperiodic flowering
CONSTANS
Posttranslational modification
Protein stability
FKBP12
topic Floral transition
Photoperiodic flowering
CONSTANS
Posttranslational modification
Protein stability
FKBP12
description Flowering time is a key process in plant development. Photoperiodic signals play a crucial role in the floral transition in Arabidopsis thaliana, and the protein CONSTANS (CO) has a central regulatory function that is tightly regulated at the transcriptional and post-translational levels. The stability of CO protein depends on a light-driven proteasome process that optimizes its accumulation in the evening to promote the production of the florigen FLOWERING LOCUS T (FT) and induce seasonal flowering. To further investigate the post-translational regulation of CO protein we have dissected its interactome network employing in vivo and in vitro assays and molecular genetics approaches. The immunophilin FKBP12 has been identified in Arabidopsis as a CO interactor that regulates its accumulation and activity. FKBP12 and CO interact through the CCT domain, affecting the stability and function of CO. fkbp12 insertion mutants show a delay in flowering time, while FKBP12 overexpression accelerates flowering, and these phenotypes can be directly related to a change in accumulation of FT protein. The interaction is conserved between the Chlamydomonas algal orthologs CrCO–CrFKBP12, revealing an ancient regulatory step in photoperiod regulation of plant development.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
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/10261/216533
url http://hdl.handle.net/10261/216533
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1111/tpj.14590
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Blackwell Publishing
publisher.none.fl_str_mv Blackwell Publishing
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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score 15,81155

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