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GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif
The activity of intracellular plant nucleotide-binding leucine-rich repeat (NB-LRR) immune receptors is fine-tuned by interactions between the receptors and their partners. Identifying NB-LRR interacting proteins is therefore crucial to advance our understanding of how these receptors function. A co...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157115/ https://www.ncbi.nlm.nih.gov/pubmed/35218353 http://dx.doi.org/10.1093/plphys/kiac081 |
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author | Sukarta, Octavina C A Zheng, Qi Slootweg, Erik J Mekken, Mark Mendel, Melanie Putker, Vera Bertran, André Brand, Anouk Overmars, Hein Pomp, Rikus Roosien, Jan Boeren, Sjef Smant, Geert Goverse, Aska |
author_facet | Sukarta, Octavina C A Zheng, Qi Slootweg, Erik J Mekken, Mark Mendel, Melanie Putker, Vera Bertran, André Brand, Anouk Overmars, Hein Pomp, Rikus Roosien, Jan Boeren, Sjef Smant, Geert Goverse, Aska |
author_sort | Sukarta, Octavina C A |
collection | PubMed |
description | The activity of intracellular plant nucleotide-binding leucine-rich repeat (NB-LRR) immune receptors is fine-tuned by interactions between the receptors and their partners. Identifying NB-LRR interacting proteins is therefore crucial to advance our understanding of how these receptors function. A co-immunoprecipitation/mass spectrometry screening was performed in Nicotiana benthamiana to identify host proteins associated with the resistance protein Gpa2, a CC-NB-LRR immune receptor conferring resistance against the potato cyst nematode Globodera pallida. A combination of biochemical, cellular, and functional assays was used to assess the role of a candidate interactor in defense. A N. benthamiana homolog of the GLYCINE-RICH RNA-BINDING PROTEIN7 (NbGRP7) protein was prioritized as a Gpa2-interacting protein for further investigations. NbGRP7 also associates in planta with the homologous Rx1 receptor, which confers immunity to Potato Virus X. We show that NbGRP7 positively regulates extreme resistance by Rx1 and cell death by Gpa2. Mutating the NbGRP7 RNA recognition motif (RRM) compromises its role in Rx1-mediated defense. Strikingly, ectopic NbGRP7 expression is likely to impact the steady-state levels of Rx1, which relies on an intact RRM. Our findings illustrate that NbGRP7 is a pro-immune component in effector-triggered immunity by regulating Gpa2/Rx1 function at a posttranscriptional level. |
format | Online Article Text |
id | pubmed-9157115 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-91571152022-06-04 GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif Sukarta, Octavina C A Zheng, Qi Slootweg, Erik J Mekken, Mark Mendel, Melanie Putker, Vera Bertran, André Brand, Anouk Overmars, Hein Pomp, Rikus Roosien, Jan Boeren, Sjef Smant, Geert Goverse, Aska Plant Physiol Research Articles The activity of intracellular plant nucleotide-binding leucine-rich repeat (NB-LRR) immune receptors is fine-tuned by interactions between the receptors and their partners. Identifying NB-LRR interacting proteins is therefore crucial to advance our understanding of how these receptors function. A co-immunoprecipitation/mass spectrometry screening was performed in Nicotiana benthamiana to identify host proteins associated with the resistance protein Gpa2, a CC-NB-LRR immune receptor conferring resistance against the potato cyst nematode Globodera pallida. A combination of biochemical, cellular, and functional assays was used to assess the role of a candidate interactor in defense. A N. benthamiana homolog of the GLYCINE-RICH RNA-BINDING PROTEIN7 (NbGRP7) protein was prioritized as a Gpa2-interacting protein for further investigations. NbGRP7 also associates in planta with the homologous Rx1 receptor, which confers immunity to Potato Virus X. We show that NbGRP7 positively regulates extreme resistance by Rx1 and cell death by Gpa2. Mutating the NbGRP7 RNA recognition motif (RRM) compromises its role in Rx1-mediated defense. Strikingly, ectopic NbGRP7 expression is likely to impact the steady-state levels of Rx1, which relies on an intact RRM. Our findings illustrate that NbGRP7 is a pro-immune component in effector-triggered immunity by regulating Gpa2/Rx1 function at a posttranscriptional level. Oxford University Press 2022-02-26 /pmc/articles/PMC9157115/ /pubmed/35218353 http://dx.doi.org/10.1093/plphys/kiac081 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Articles Sukarta, Octavina C A Zheng, Qi Slootweg, Erik J Mekken, Mark Mendel, Melanie Putker, Vera Bertran, André Brand, Anouk Overmars, Hein Pomp, Rikus Roosien, Jan Boeren, Sjef Smant, Geert Goverse, Aska GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif |
title | GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif |
title_full | GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif |
title_fullStr | GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif |
title_full_unstemmed | GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif |
title_short | GLYCINE-RICH RNA-BINDING PROTEIN 7 potentiates effector-triggered immunity through an RNA recognition motif |
title_sort | glycine-rich rna-binding protein 7 potentiates effector-triggered immunity through an rna recognition motif |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157115/ https://www.ncbi.nlm.nih.gov/pubmed/35218353 http://dx.doi.org/10.1093/plphys/kiac081 |
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