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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/271599
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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 Técnicas2025-09-29T09:43:30Zoai: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:34982025-09-29 09:43:30.981CONICET 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 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión Journal http://purl.org/coar/resource_type/c_5794 info:ar-repo/semantics/documentoDeConferencia |
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publishedVersion |
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conferenceObject |
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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 |
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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 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
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