Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites

Autores
Peralta, Diego Alberto; Araya, Alejandro; Nardi, Cristina Fernanda; Busi, María Victoria; Gomez Casati, Diego Fabian
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein ubiquitination leading to degradation by the proteasome is an important mechanism in regulating key cellular functions. Protein ubiquitination is carried out by a three step process involving ubiquitin (Ub) activation by a E1 enzyme, the transfer of Ub to a protein E2, finally an ubiquitin ligase E3 catalyzes the transfer of the Ub peptide to an acceptor protein. The E3 component is responsible for the specific recognition of the target, making the unveiling of E3 components essential to understand the mechanisms regulating fundamental cell processes through the protein degradation pathways. The Arabidopsis thaliana seven in absentia-like 7 (AtSINAL7) gene encodes for a protein with characteristics from a C3HC4-type E3 ubiquitin ligase. We demonstrate here that AtSINAL7 protein is indeed an E3 protein ligase based on the self-ubiquitination in vitro assay. This activity is dependent of the presence of a Lys residue in position 124. We also found that higher AtSINAL7 transcript levels are present in tissues undergoing active cell division during floral development. An interesting observation is the circadian expression pattern of AtSINAL7 mRNA in floral buds. Furthermore, UV–B irradiation induces the expression of this transcript indicating that AtSINAL7 may be involved in a wide range of different cell processes.
Fil: Peralta, Diego Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina
Fil: Araya, Alejandro. Centre National de la Recherche Scientifique; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Nardi, Cristina Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina
Materia
AtSINAL7
Arabidopsis
Seven in absentia
Ubiquitination
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/26390
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/26390
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sitesPeralta, Diego AlbertoAraya, AlejandroNardi, Cristina FernandaBusi, María VictoriaGomez Casati, Diego FabianAtSINAL7ArabidopsisSeven in absentiaUbiquitinationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Protein ubiquitination leading to degradation by the proteasome is an important mechanism in regulating key cellular functions. Protein ubiquitination is carried out by a three step process involving ubiquitin (Ub) activation by a E1 enzyme, the transfer of Ub to a protein E2, finally an ubiquitin ligase E3 catalyzes the transfer of the Ub peptide to an acceptor protein. The E3 component is responsible for the specific recognition of the target, making the unveiling of E3 components essential to understand the mechanisms regulating fundamental cell processes through the protein degradation pathways. The Arabidopsis thaliana seven in absentia-like 7 (AtSINAL7) gene encodes for a protein with characteristics from a C3HC4-type E3 ubiquitin ligase. We demonstrate here that AtSINAL7 protein is indeed an E3 protein ligase based on the self-ubiquitination in vitro assay. This activity is dependent of the presence of a Lys residue in position 124. We also found that higher AtSINAL7 transcript levels are present in tissues undergoing active cell division during floral development. An interesting observation is the circadian expression pattern of AtSINAL7 mRNA in floral buds. Furthermore, UV–B irradiation induces the expression of this transcript indicating that AtSINAL7 may be involved in a wide range of different cell processes.Fil: Peralta, Diego Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; ArgentinaFil: Araya, Alejandro. Centre National de la Recherche Scientifique; Francia. Institut National de la Recherche Agronomique; FranciaFil: Nardi, Cristina Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; ArgentinaPublic Library Science2013-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26390Peralta, Diego Alberto; Araya, Alejandro; Nardi, Cristina Fernanda; Busi, María Victoria; Gomez Casati, Diego Fabian; Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites; Public Library Science; Plos One; 8; 8; 8-2013; 1-10; e7311932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0073104info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0073104info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3756039/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:00:08Zoai:ri.conicet.gov.ar:11336/26390instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 12:00:08.995CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
title Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
spellingShingle Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
Peralta, Diego Alberto
AtSINAL7
Arabidopsis
Seven in absentia
Ubiquitination
title_short Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
title_full Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
title_fullStr Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
title_full_unstemmed Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
title_sort Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites
dc.creator.none.fl_str_mv Peralta, Diego Alberto
Araya, Alejandro
Nardi, Cristina Fernanda
Busi, María Victoria
Gomez Casati, Diego Fabian
author Peralta, Diego Alberto
author_facet Peralta, Diego Alberto
Araya, Alejandro
Nardi, Cristina Fernanda
Busi, María Victoria
Gomez Casati, Diego Fabian
author_role author
author2 Araya, Alejandro
Nardi, Cristina Fernanda
Busi, María Victoria
Gomez Casati, Diego Fabian
author2_role author
author
author
author
dc.subject.none.fl_str_mv AtSINAL7
Arabidopsis
Seven in absentia
Ubiquitination
topic AtSINAL7
Arabidopsis
Seven in absentia
Ubiquitination
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Protein ubiquitination leading to degradation by the proteasome is an important mechanism in regulating key cellular functions. Protein ubiquitination is carried out by a three step process involving ubiquitin (Ub) activation by a E1 enzyme, the transfer of Ub to a protein E2, finally an ubiquitin ligase E3 catalyzes the transfer of the Ub peptide to an acceptor protein. The E3 component is responsible for the specific recognition of the target, making the unveiling of E3 components essential to understand the mechanisms regulating fundamental cell processes through the protein degradation pathways. The Arabidopsis thaliana seven in absentia-like 7 (AtSINAL7) gene encodes for a protein with characteristics from a C3HC4-type E3 ubiquitin ligase. We demonstrate here that AtSINAL7 protein is indeed an E3 protein ligase based on the self-ubiquitination in vitro assay. This activity is dependent of the presence of a Lys residue in position 124. We also found that higher AtSINAL7 transcript levels are present in tissues undergoing active cell division during floral development. An interesting observation is the circadian expression pattern of AtSINAL7 mRNA in floral buds. Furthermore, UV–B irradiation induces the expression of this transcript indicating that AtSINAL7 may be involved in a wide range of different cell processes.
Fil: Peralta, Diego Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina
Fil: Araya, Alejandro. Centre National de la Recherche Scientifique; Francia. Institut National de la Recherche Agronomique; Francia
Fil: Nardi, Cristina Fernanda. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Centro de Estudios Fotosinteticos y Bioquimicos. Universidad Nacional de Rosario. Facultad de Cs.bioquímicas y Farmaceuticas. Centro de Estudios Fotosinteticos y Bioquimicos; Argentina
description Protein ubiquitination leading to degradation by the proteasome is an important mechanism in regulating key cellular functions. Protein ubiquitination is carried out by a three step process involving ubiquitin (Ub) activation by a E1 enzyme, the transfer of Ub to a protein E2, finally an ubiquitin ligase E3 catalyzes the transfer of the Ub peptide to an acceptor protein. The E3 component is responsible for the specific recognition of the target, making the unveiling of E3 components essential to understand the mechanisms regulating fundamental cell processes through the protein degradation pathways. The Arabidopsis thaliana seven in absentia-like 7 (AtSINAL7) gene encodes for a protein with characteristics from a C3HC4-type E3 ubiquitin ligase. We demonstrate here that AtSINAL7 protein is indeed an E3 protein ligase based on the self-ubiquitination in vitro assay. This activity is dependent of the presence of a Lys residue in position 124. We also found that higher AtSINAL7 transcript levels are present in tissues undergoing active cell division during floral development. An interesting observation is the circadian expression pattern of AtSINAL7 mRNA in floral buds. Furthermore, UV–B irradiation induces the expression of this transcript indicating that AtSINAL7 may be involved in a wide range of different cell processes.
publishDate 2013
dc.date.none.fl_str_mv 2013-08
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/11336/26390
Peralta, Diego Alberto; Araya, Alejandro; Nardi, Cristina Fernanda; Busi, María Victoria; Gomez Casati, Diego Fabian; Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites; Public Library Science; Plos One; 8; 8; 8-2013; 1-10; e731
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/26390
identifier_str_mv Peralta, Diego Alberto; Araya, Alejandro; Nardi, Cristina Fernanda; Busi, María Victoria; Gomez Casati, Diego Fabian; Characterization of the Arabidopsis thaliana E3 Ubiquitin-Ligase AtSINAL7 and identification of the Ubiquitination sites; Public Library Science; Plos One; 8; 8; 8-2013; 1-10; e731
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0073104
info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0073104
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3756039/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Public Library Science
publisher.none.fl_str_mv Public Library Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.234792

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