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Protein-protein interactions in the RPS4/RRS1 immune receptor complex
Plant NLR (Nucleotide-binding domain and Leucine-rich Repeat) immune receptor proteins are encoded by Resistance (R) genes and confer specific resistance to pathogen races that carry the corresponding recognized effectors. Some NLR proteins function in pairs, forming receptor complexes for the perce...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5435354/ https://www.ncbi.nlm.nih.gov/pubmed/28475615 http://dx.doi.org/10.1371/journal.ppat.1006376 |
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author | Huh, Sung Un Cevik, Volkan Ding, Pingtao Duxbury, Zane Ma, Yan Tomlinson, Laurence Sarris, Panagiotis F. Jones, Jonathan D. G. |
author_facet | Huh, Sung Un Cevik, Volkan Ding, Pingtao Duxbury, Zane Ma, Yan Tomlinson, Laurence Sarris, Panagiotis F. Jones, Jonathan D. G. |
author_sort | Huh, Sung Un |
collection | PubMed |
description | Plant NLR (Nucleotide-binding domain and Leucine-rich Repeat) immune receptor proteins are encoded by Resistance (R) genes and confer specific resistance to pathogen races that carry the corresponding recognized effectors. Some NLR proteins function in pairs, forming receptor complexes for the perception of specific effectors. We show here that the Arabidopsis RPS4 and RRS1 NLR proteins are both required to make an authentic immune complex. Over-expression of RPS4 in tobacco or in Arabidopsis results in constitutive defense activation; this phenotype is suppressed in the presence of RRS1. RRS1 protein co-immunoprecipitates (co-IPs) with itself in the presence or absence of RPS4, but in contrast, RPS4 does not associate with itself in the absence of RRS1. In the presence of RRS1, RPS4 associates with defense signaling regulator EDS1 solely in the nucleus, in contrast to the extra-nuclear location found in the absence of RRS1. The AvrRps4 effector does not disrupt RPS4-EDS1 association in the presence of RRS1. In the absence of RRS1, AvrRps4 interacts with EDS1, forming nucleocytoplasmic aggregates, the formation of which is disturbed by the co-expression of PAD4 but not by SAG101. These data indicate that the study of an immune receptor protein complex in the absence of all components can result in misleading inferences, and reveals an NLR complex that dynamically interacts with the immune regulators EDS1/PAD4 or EDS1/SAG101, and with effectors, during the process by which effector recognition is converted to defense activation. |
format | Online Article Text |
id | pubmed-5435354 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-54353542017-05-26 Protein-protein interactions in the RPS4/RRS1 immune receptor complex Huh, Sung Un Cevik, Volkan Ding, Pingtao Duxbury, Zane Ma, Yan Tomlinson, Laurence Sarris, Panagiotis F. Jones, Jonathan D. G. PLoS Pathog Research Article Plant NLR (Nucleotide-binding domain and Leucine-rich Repeat) immune receptor proteins are encoded by Resistance (R) genes and confer specific resistance to pathogen races that carry the corresponding recognized effectors. Some NLR proteins function in pairs, forming receptor complexes for the perception of specific effectors. We show here that the Arabidopsis RPS4 and RRS1 NLR proteins are both required to make an authentic immune complex. Over-expression of RPS4 in tobacco or in Arabidopsis results in constitutive defense activation; this phenotype is suppressed in the presence of RRS1. RRS1 protein co-immunoprecipitates (co-IPs) with itself in the presence or absence of RPS4, but in contrast, RPS4 does not associate with itself in the absence of RRS1. In the presence of RRS1, RPS4 associates with defense signaling regulator EDS1 solely in the nucleus, in contrast to the extra-nuclear location found in the absence of RRS1. The AvrRps4 effector does not disrupt RPS4-EDS1 association in the presence of RRS1. In the absence of RRS1, AvrRps4 interacts with EDS1, forming nucleocytoplasmic aggregates, the formation of which is disturbed by the co-expression of PAD4 but not by SAG101. These data indicate that the study of an immune receptor protein complex in the absence of all components can result in misleading inferences, and reveals an NLR complex that dynamically interacts with the immune regulators EDS1/PAD4 or EDS1/SAG101, and with effectors, during the process by which effector recognition is converted to defense activation. Public Library of Science 2017-05-05 /pmc/articles/PMC5435354/ /pubmed/28475615 http://dx.doi.org/10.1371/journal.ppat.1006376 Text en © 2017 Huh et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Huh, Sung Un Cevik, Volkan Ding, Pingtao Duxbury, Zane Ma, Yan Tomlinson, Laurence Sarris, Panagiotis F. Jones, Jonathan D. G. Protein-protein interactions in the RPS4/RRS1 immune receptor complex |
title | Protein-protein interactions in the RPS4/RRS1 immune receptor complex |
title_full | Protein-protein interactions in the RPS4/RRS1 immune receptor complex |
title_fullStr | Protein-protein interactions in the RPS4/RRS1 immune receptor complex |
title_full_unstemmed | Protein-protein interactions in the RPS4/RRS1 immune receptor complex |
title_short | Protein-protein interactions in the RPS4/RRS1 immune receptor complex |
title_sort | protein-protein interactions in the rps4/rrs1 immune receptor complex |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5435354/ https://www.ncbi.nlm.nih.gov/pubmed/28475615 http://dx.doi.org/10.1371/journal.ppat.1006376 |
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