Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription

Autores
Iñigo, S.; Giraldez, A.N.; Chory, J.; Cerdán, P.D.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The Mediator complex is a greater than 1-megadalton complex, composed of about 30 subunits and found in most eukaryotes, whose main role is to transmit signals from DNA-bound transcription factors to RNA Polymerase II. The proteasome is emerging as an important regulator of transcription during both initiation and elongation. It is increasing the number of cases where the proteolysis of transcriptional activators by the proteasome activates their function. This counterintuitive phenomenon was called "activation by destruction." Here, we show that, in Arabidopsis (Arabidopsis thaliana), PHYTOCHROME AND FLOWERING TIME1 (PFT1), the MEDIATOR25 (MED25) subunit of the plant Mediator complex, is degraded by the proteasome and that proteasome-mediated PFT1 turnover is coupled to its role in stimulating the transcription of FLOWERING LOCUS T, the plant florigen, which is involved in the process of flowering induction. We further identify two novel RING-H2 proteins that target PFT1 for degradation. We show that MED25-BINDING RING-H2 PROTEIN1 (MBR1) and MBR2 bind to PFT1 in yeast (Saccharomyces cerevisiae) and in vitro, and they promote PFT1 degradation in vivo, in a RING-H2- dependent way, typical of E3 ubiquitin ligases. We further show that both MBR1 and MBR2 also promote flowering by PFT1- dependent and -independent mechanisms. Our findings extend the phenomenon of activation by destruction to a Mediator subunit, adding a new mechanism by which Mediator subunits may regulate downstream genes in specific pathways. Furthermore, we show that two novel RING-H2 proteins are involved in the destruction of PFT1, adding new players to this process in plants. © 2012 American Society of Plant Biologists.
Fil:Cerdán, P.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Plant Physiol. 2012;160(3):1662-1673
Materia
Arabidopsis protein
FT protein, Arabidopsis
nuclear protein
PFT1 protein, Arabidopsis
proteasome
ubiquitin protein ligase
amino acid sequence
Arabidopsis
article
chemistry
flower
gene expression regulation
gene silencing
genetic transcription
genetics
metabolism
molecular genetics
mutation
physiology
protein binding
protein degradation
protein stability
protein tertiary structure
Amino Acid Sequence
Arabidopsis
Arabidopsis Proteins
Flowers
Gene Expression Regulation, Plant
Gene Knockdown Techniques
Molecular Sequence Data
Mutation
Nuclear Proteins
Proteasome Endopeptidase Complex
Protein Binding
Protein Stability
Protein Structure, Tertiary
Proteolysis
Transcription, Genetic
Ubiquitin-Protein Ligases
Arabidopsis
Arabidopsis thaliana
Eukaryota
Saccharomyces cerevisiae
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00320889_v160_n3_p1662_Inigo

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oai_identifier_str paperaa:paper_00320889_v160_n3_p1662_Inigo
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcriptionIñigo, S.Giraldez, A.N.Chory, J.Cerdán, P.D.Arabidopsis proteinFT protein, Arabidopsisnuclear proteinPFT1 protein, Arabidopsisproteasomeubiquitin protein ligaseamino acid sequenceArabidopsisarticlechemistryflowergene expression regulationgene silencinggenetic transcriptiongeneticsmetabolismmolecular geneticsmutationphysiologyprotein bindingprotein degradationprotein stabilityprotein tertiary structureAmino Acid SequenceArabidopsisArabidopsis ProteinsFlowersGene Expression Regulation, PlantGene Knockdown TechniquesMolecular Sequence DataMutationNuclear ProteinsProteasome Endopeptidase ComplexProtein BindingProtein StabilityProtein Structure, TertiaryProteolysisTranscription, GeneticUbiquitin-Protein LigasesArabidopsisArabidopsis thalianaEukaryotaSaccharomyces cerevisiaeThe Mediator complex is a greater than 1-megadalton complex, composed of about 30 subunits and found in most eukaryotes, whose main role is to transmit signals from DNA-bound transcription factors to RNA Polymerase II. The proteasome is emerging as an important regulator of transcription during both initiation and elongation. It is increasing the number of cases where the proteolysis of transcriptional activators by the proteasome activates their function. This counterintuitive phenomenon was called "activation by destruction." Here, we show that, in Arabidopsis (Arabidopsis thaliana), PHYTOCHROME AND FLOWERING TIME1 (PFT1), the MEDIATOR25 (MED25) subunit of the plant Mediator complex, is degraded by the proteasome and that proteasome-mediated PFT1 turnover is coupled to its role in stimulating the transcription of FLOWERING LOCUS T, the plant florigen, which is involved in the process of flowering induction. We further identify two novel RING-H2 proteins that target PFT1 for degradation. We show that MED25-BINDING RING-H2 PROTEIN1 (MBR1) and MBR2 bind to PFT1 in yeast (Saccharomyces cerevisiae) and in vitro, and they promote PFT1 degradation in vivo, in a RING-H2- dependent way, typical of E3 ubiquitin ligases. We further show that both MBR1 and MBR2 also promote flowering by PFT1- dependent and -independent mechanisms. Our findings extend the phenomenon of activation by destruction to a Mediator subunit, adding a new mechanism by which Mediator subunits may regulate downstream genes in specific pathways. Furthermore, we show that two novel RING-H2 proteins are involved in the destruction of PFT1, adding new players to this process in plants. © 2012 American Society of Plant Biologists.Fil:Cerdán, P.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00320889_v160_n3_p1662_InigoPlant Physiol. 2012;160(3):1662-1673reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:05Zpaperaa:paper_00320889_v160_n3_p1662_InigoInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:07.203Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
title Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
spellingShingle Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
Iñigo, S.
Arabidopsis protein
FT protein, Arabidopsis
nuclear protein
PFT1 protein, Arabidopsis
proteasome
ubiquitin protein ligase
amino acid sequence
Arabidopsis
article
chemistry
flower
gene expression regulation
gene silencing
genetic transcription
genetics
metabolism
molecular genetics
mutation
physiology
protein binding
protein degradation
protein stability
protein tertiary structure
Amino Acid Sequence
Arabidopsis
Arabidopsis Proteins
Flowers
Gene Expression Regulation, Plant
Gene Knockdown Techniques
Molecular Sequence Data
Mutation
Nuclear Proteins
Proteasome Endopeptidase Complex
Protein Binding
Protein Stability
Protein Structure, Tertiary
Proteolysis
Transcription, Genetic
Ubiquitin-Protein Ligases
Arabidopsis
Arabidopsis thaliana
Eukaryota
Saccharomyces cerevisiae
title_short Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
title_full Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
title_fullStr Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
title_full_unstemmed Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
title_sort Proteasome-mediated turnover of arabidopsis MED25 is coupled to the activation of FLOWERING LOCUS T transcription
dc.creator.none.fl_str_mv Iñigo, S.
Giraldez, A.N.
Chory, J.
Cerdán, P.D.
author Iñigo, S.
author_facet Iñigo, S.
Giraldez, A.N.
Chory, J.
Cerdán, P.D.
author_role author
author2 Giraldez, A.N.
Chory, J.
Cerdán, P.D.
author2_role author
author
author
dc.subject.none.fl_str_mv Arabidopsis protein
FT protein, Arabidopsis
nuclear protein
PFT1 protein, Arabidopsis
proteasome
ubiquitin protein ligase
amino acid sequence
Arabidopsis
article
chemistry
flower
gene expression regulation
gene silencing
genetic transcription
genetics
metabolism
molecular genetics
mutation
physiology
protein binding
protein degradation
protein stability
protein tertiary structure
Amino Acid Sequence
Arabidopsis
Arabidopsis Proteins
Flowers
Gene Expression Regulation, Plant
Gene Knockdown Techniques
Molecular Sequence Data
Mutation
Nuclear Proteins
Proteasome Endopeptidase Complex
Protein Binding
Protein Stability
Protein Structure, Tertiary
Proteolysis
Transcription, Genetic
Ubiquitin-Protein Ligases
Arabidopsis
Arabidopsis thaliana
Eukaryota
Saccharomyces cerevisiae
topic Arabidopsis protein
FT protein, Arabidopsis
nuclear protein
PFT1 protein, Arabidopsis
proteasome
ubiquitin protein ligase
amino acid sequence
Arabidopsis
article
chemistry
flower
gene expression regulation
gene silencing
genetic transcription
genetics
metabolism
molecular genetics
mutation
physiology
protein binding
protein degradation
protein stability
protein tertiary structure
Amino Acid Sequence
Arabidopsis
Arabidopsis Proteins
Flowers
Gene Expression Regulation, Plant
Gene Knockdown Techniques
Molecular Sequence Data
Mutation
Nuclear Proteins
Proteasome Endopeptidase Complex
Protein Binding
Protein Stability
Protein Structure, Tertiary
Proteolysis
Transcription, Genetic
Ubiquitin-Protein Ligases
Arabidopsis
Arabidopsis thaliana
Eukaryota
Saccharomyces cerevisiae
dc.description.none.fl_txt_mv The Mediator complex is a greater than 1-megadalton complex, composed of about 30 subunits and found in most eukaryotes, whose main role is to transmit signals from DNA-bound transcription factors to RNA Polymerase II. The proteasome is emerging as an important regulator of transcription during both initiation and elongation. It is increasing the number of cases where the proteolysis of transcriptional activators by the proteasome activates their function. This counterintuitive phenomenon was called "activation by destruction." Here, we show that, in Arabidopsis (Arabidopsis thaliana), PHYTOCHROME AND FLOWERING TIME1 (PFT1), the MEDIATOR25 (MED25) subunit of the plant Mediator complex, is degraded by the proteasome and that proteasome-mediated PFT1 turnover is coupled to its role in stimulating the transcription of FLOWERING LOCUS T, the plant florigen, which is involved in the process of flowering induction. We further identify two novel RING-H2 proteins that target PFT1 for degradation. We show that MED25-BINDING RING-H2 PROTEIN1 (MBR1) and MBR2 bind to PFT1 in yeast (Saccharomyces cerevisiae) and in vitro, and they promote PFT1 degradation in vivo, in a RING-H2- dependent way, typical of E3 ubiquitin ligases. We further show that both MBR1 and MBR2 also promote flowering by PFT1- dependent and -independent mechanisms. Our findings extend the phenomenon of activation by destruction to a Mediator subunit, adding a new mechanism by which Mediator subunits may regulate downstream genes in specific pathways. Furthermore, we show that two novel RING-H2 proteins are involved in the destruction of PFT1, adding new players to this process in plants. © 2012 American Society of Plant Biologists.
Fil:Cerdán, P.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description The Mediator complex is a greater than 1-megadalton complex, composed of about 30 subunits and found in most eukaryotes, whose main role is to transmit signals from DNA-bound transcription factors to RNA Polymerase II. The proteasome is emerging as an important regulator of transcription during both initiation and elongation. It is increasing the number of cases where the proteolysis of transcriptional activators by the proteasome activates their function. This counterintuitive phenomenon was called "activation by destruction." Here, we show that, in Arabidopsis (Arabidopsis thaliana), PHYTOCHROME AND FLOWERING TIME1 (PFT1), the MEDIATOR25 (MED25) subunit of the plant Mediator complex, is degraded by the proteasome and that proteasome-mediated PFT1 turnover is coupled to its role in stimulating the transcription of FLOWERING LOCUS T, the plant florigen, which is involved in the process of flowering induction. We further identify two novel RING-H2 proteins that target PFT1 for degradation. We show that MED25-BINDING RING-H2 PROTEIN1 (MBR1) and MBR2 bind to PFT1 in yeast (Saccharomyces cerevisiae) and in vitro, and they promote PFT1 degradation in vivo, in a RING-H2- dependent way, typical of E3 ubiquitin ligases. We further show that both MBR1 and MBR2 also promote flowering by PFT1- dependent and -independent mechanisms. Our findings extend the phenomenon of activation by destruction to a Mediator subunit, adding a new mechanism by which Mediator subunits may regulate downstream genes in specific pathways. Furthermore, we show that two novel RING-H2 proteins are involved in the destruction of PFT1, adding new players to this process in plants. © 2012 American Society of Plant Biologists.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_00320889_v160_n3_p1662_Inigo
url http://hdl.handle.net/20.500.12110/paper_00320889_v160_n3_p1662_Inigo
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Plant Physiol. 2012;160(3):1662-1673
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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