Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids

Autores
Peppino Margutti, Micaela Yesica; Merino, Gabriela Alejandra; Alvarez, Maria Elena; Cecchini, Nicolas Miguel
Año de publicación
2020
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Plants depend on a non-adaptive immune system triggered by receptors after the detection of pathogens. Among them, nucleotide-binding leucine-rich repeat receptors (NLRs) family are key immune sensors that recognize specific effectors used by pathogens to promote their virulence. NLR proteins have been found in various subcellular compartments and they can be relocated after activation, indicating that trafficking is involved in their function. However, NLRs acting from endosymbiont organelles such as plastids or mitochondria have not been described. NLRs consist of a N-terminal region that is similar to the "Toll/Interleukin-1 receptor" (TIR) or forms a "coiled coil" (CC), a nucleotide binding domain (NB) and a leucine rich repeat (LRR) (TIR/CC-NB-LRR). Recently, we have found a novel N-terminal localization signal for plastid or mitochondria targeting. Notably, among the Arabidopsis predicted proteins that possess this signature one is the NLR receptor BNT1. In this work, we have characterized the changes in transcripts and localization of BNT1. We carried out an in silico analysis of the transcriptional variations of BNT1 isoforms generated by alternative splicing (AS). By RT-PCR we validated and examined the BNT1 isoforms level in basal and biotic/abiotic stress conditions. We also generated BNT1-GFP fusions for transient expression in Nicotiana benthamiana to determine its localization using confocal microscopy and subcellular fractionations. Several BNT1 N-terminal mutated versions were also analyzed. Together, our results suggest that BNT1 isoforms generated by AS specifically participate in different stress responses. Additionally, the differential localization of BNT1 mutated versions suggest a key role of its N-terminal region during defenses against pathogens. The elucidation of BNT1 biological role could represent a paradigm to understand the function of NLR immune receptors localized in plastids and different subcellular spaces.
Fil: Peppino Margutti, Micaela Yesica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Merino, Gabriela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Alvarez, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Cecchini, Nicolas Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
IV Reunión Conjunta de Sociedades de Biología de la República Argentina; XXXVIII Reunión Anual de la Sociedad de Biología de Cuyo; XXIII Reunión Anual de la Sociedad de Biología de Córdoba; XXXVII Reunión Anual de la Sociedad de Biología de Tucumán: Nuevas Evidencias y Cambios de Paradigmas en Ciencias Biológicas
Virtual
Argentina
Sociedad de Biología de Cuyo
Sociedad de Biología de Córdoba
Sociedad de Biología de Rosario
Asociación de Biología de Tucumán
Materia
Plant
Pathogens
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:11336/271599
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastidsPeppino Margutti, Micaela YesicaMerino, Gabriela AlejandraAlvarez, Maria ElenaCecchini, Nicolas MiguelPlantPathogenshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plants depend on a non-adaptive immune system triggered by receptors after the detection of pathogens. Among them, nucleotide-binding leucine-rich repeat receptors (NLRs) family are key immune sensors that recognize specific effectors used by pathogens to promote their virulence. NLR proteins have been found in various subcellular compartments and they can be relocated after activation, indicating that trafficking is involved in their function. However, NLRs acting from endosymbiont organelles such as plastids or mitochondria have not been described. NLRs consist of a N-terminal region that is similar to the "Toll/Interleukin-1 receptor" (TIR) or forms a "coiled coil" (CC), a nucleotide binding domain (NB) and a leucine rich repeat (LRR) (TIR/CC-NB-LRR). Recently, we have found a novel N-terminal localization signal for plastid or mitochondria targeting. Notably, among the Arabidopsis predicted proteins that possess this signature one is the NLR receptor BNT1. In this work, we have characterized the changes in transcripts and localization of BNT1. We carried out an in silico analysis of the transcriptional variations of BNT1 isoforms generated by alternative splicing (AS). By RT-PCR we validated and examined the BNT1 isoforms level in basal and biotic/abiotic stress conditions. We also generated BNT1-GFP fusions for transient expression in Nicotiana benthamiana to determine its localization using confocal microscopy and subcellular fractionations. Several BNT1 N-terminal mutated versions were also analyzed. Together, our results suggest that BNT1 isoforms generated by AS specifically participate in different stress responses. Additionally, the differential localization of BNT1 mutated versions suggest a key role of its N-terminal region during defenses against pathogens. The elucidation of BNT1 biological role could represent a paradigm to understand the function of NLR immune receptors localized in plastids and different subcellular spaces.Fil: Peppino Margutti, Micaela Yesica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Merino, Gabriela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Alvarez, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Cecchini, Nicolas Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaIV Reunión Conjunta de Sociedades de Biología de la República Argentina; XXXVIII Reunión Anual de la Sociedad de Biología de Cuyo; XXIII Reunión Anual de la Sociedad de Biología de Córdoba; XXXVII Reunión Anual de la Sociedad de Biología de Tucumán: Nuevas Evidencias y Cambios de Paradigmas en Ciencias BiológicasVirtualArgentinaSociedad de Biología de CuyoSociedad de Biología de CórdobaSociedad de Biología de RosarioAsociación de Biología de TucumánTech Science Press2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/271599Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids; IV Reunión Conjunta de Sociedades de Biología de la República Argentina; XXXVIII Reunión Anual de la Sociedad de Biología de Cuyo; XXIII Reunión Anual de la Sociedad de Biología de Córdoba; XXXVII Reunión Anual de la Sociedad de Biología de Tucumán: Nuevas Evidencias y Cambios de Paradigmas en Ciencias Biológicas; Virtual; Argentina; 2020; 80-800327-95451667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://sbcuyo.org.ar/reuniones-anuales-anteriores/info:eu-repo/semantics/altIdentifier/url/https://sbcuyo.org.ar/wp-content/uploads/2021/08/BIOCELL-Vol_-45-Suppl_-3-2021.pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:36:47Zoai:ri.conicet.gov.ar:11336/271599instacron: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:34982025-10-15 14:36:48.069CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
title Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
spellingShingle Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
Peppino Margutti, Micaela Yesica
Plant
Pathogens
title_short Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
title_full Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
title_fullStr Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
title_full_unstemmed Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
title_sort Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids
dc.creator.none.fl_str_mv Peppino Margutti, Micaela Yesica
Merino, Gabriela Alejandra
Alvarez, Maria Elena
Cecchini, Nicolas Miguel
author Peppino Margutti, Micaela Yesica
author_facet Peppino Margutti, Micaela Yesica
Merino, Gabriela Alejandra
Alvarez, Maria Elena
Cecchini, Nicolas Miguel
author_role author
author2 Merino, Gabriela Alejandra
Alvarez, Maria Elena
Cecchini, Nicolas Miguel
author2_role author
author
author
dc.subject.none.fl_str_mv Plant
Pathogens
topic Plant
Pathogens
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plants depend on a non-adaptive immune system triggered by receptors after the detection of pathogens. Among them, nucleotide-binding leucine-rich repeat receptors (NLRs) family are key immune sensors that recognize specific effectors used by pathogens to promote their virulence. NLR proteins have been found in various subcellular compartments and they can be relocated after activation, indicating that trafficking is involved in their function. However, NLRs acting from endosymbiont organelles such as plastids or mitochondria have not been described. NLRs consist of a N-terminal region that is similar to the "Toll/Interleukin-1 receptor" (TIR) or forms a "coiled coil" (CC), a nucleotide binding domain (NB) and a leucine rich repeat (LRR) (TIR/CC-NB-LRR). Recently, we have found a novel N-terminal localization signal for plastid or mitochondria targeting. Notably, among the Arabidopsis predicted proteins that possess this signature one is the NLR receptor BNT1. In this work, we have characterized the changes in transcripts and localization of BNT1. We carried out an in silico analysis of the transcriptional variations of BNT1 isoforms generated by alternative splicing (AS). By RT-PCR we validated and examined the BNT1 isoforms level in basal and biotic/abiotic stress conditions. We also generated BNT1-GFP fusions for transient expression in Nicotiana benthamiana to determine its localization using confocal microscopy and subcellular fractionations. Several BNT1 N-terminal mutated versions were also analyzed. Together, our results suggest that BNT1 isoforms generated by AS specifically participate in different stress responses. Additionally, the differential localization of BNT1 mutated versions suggest a key role of its N-terminal region during defenses against pathogens. The elucidation of BNT1 biological role could represent a paradigm to understand the function of NLR immune receptors localized in plastids and different subcellular spaces.
Fil: Peppino Margutti, Micaela Yesica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Merino, Gabriela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Alvarez, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Cecchini, Nicolas Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
IV Reunión Conjunta de Sociedades de Biología de la República Argentina; XXXVIII Reunión Anual de la Sociedad de Biología de Cuyo; XXIII Reunión Anual de la Sociedad de Biología de Córdoba; XXXVII Reunión Anual de la Sociedad de Biología de Tucumán: Nuevas Evidencias y Cambios de Paradigmas en Ciencias Biológicas
Virtual
Argentina
Sociedad de Biología de Cuyo
Sociedad de Biología de Córdoba
Sociedad de Biología de Rosario
Asociación de Biología de Tucumán
description Plants depend on a non-adaptive immune system triggered by receptors after the detection of pathogens. Among them, nucleotide-binding leucine-rich repeat receptors (NLRs) family are key immune sensors that recognize specific effectors used by pathogens to promote their virulence. NLR proteins have been found in various subcellular compartments and they can be relocated after activation, indicating that trafficking is involved in their function. However, NLRs acting from endosymbiont organelles such as plastids or mitochondria have not been described. NLRs consist of a N-terminal region that is similar to the "Toll/Interleukin-1 receptor" (TIR) or forms a "coiled coil" (CC), a nucleotide binding domain (NB) and a leucine rich repeat (LRR) (TIR/CC-NB-LRR). Recently, we have found a novel N-terminal localization signal for plastid or mitochondria targeting. Notably, among the Arabidopsis predicted proteins that possess this signature one is the NLR receptor BNT1. In this work, we have characterized the changes in transcripts and localization of BNT1. We carried out an in silico analysis of the transcriptional variations of BNT1 isoforms generated by alternative splicing (AS). By RT-PCR we validated and examined the BNT1 isoforms level in basal and biotic/abiotic stress conditions. We also generated BNT1-GFP fusions for transient expression in Nicotiana benthamiana to determine its localization using confocal microscopy and subcellular fractionations. Several BNT1 N-terminal mutated versions were also analyzed. Together, our results suggest that BNT1 isoforms generated by AS specifically participate in different stress responses. Additionally, the differential localization of BNT1 mutated versions suggest a key role of its N-terminal region during defenses against pathogens. The elucidation of BNT1 biological role could represent a paradigm to understand the function of NLR immune receptors localized in plastids and different subcellular spaces.
publishDate 2020
dc.date.none.fl_str_mv 2020
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dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/271599
Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids; IV Reunión Conjunta de Sociedades de Biología de la República Argentina; XXXVIII Reunión Anual de la Sociedad de Biología de Cuyo; XXIII Reunión Anual de la Sociedad de Biología de Córdoba; XXXVII Reunión Anual de la Sociedad de Biología de Tucumán: Nuevas Evidencias y Cambios de Paradigmas en Ciencias Biológicas; Virtual; Argentina; 2020; 80-80
0327-9545
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/271599
identifier_str_mv Characterization of the BNT1 immune receptor in Arabidopsis targeted to plastids; IV Reunión Conjunta de Sociedades de Biología de la República Argentina; XXXVIII Reunión Anual de la Sociedad de Biología de Cuyo; XXIII Reunión Anual de la Sociedad de Biología de Córdoba; XXXVII Reunión Anual de la Sociedad de Biología de Tucumán: Nuevas Evidencias y Cambios de Paradigmas en Ciencias Biológicas; Virtual; Argentina; 2020; 80-80
0327-9545
1667-5746
CONICET Digital
CONICET
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language eng
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