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...
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| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2017-05-01
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| Series: | PLoS Pathogens |
| Online Access: | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006376&type=printable |
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| author | Sung Un Huh Volkan Cevik Pingtao Ding Zane Duxbury Yan Ma Laurence Tomlinson Panagiotis F Sarris Jonathan D G Jones |
| author_facet | Sung Un Huh Volkan Cevik Pingtao Ding Zane Duxbury Yan Ma Laurence Tomlinson Panagiotis F Sarris Jonathan D G Jones |
| author_sort | Sung Un Huh |
| collection | DOAJ |
| 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 | Article |
| id | doaj-art-3a6e1ba2df1a435299099f34e68cf1aa |
| institution | OA Journals |
| issn | 1553-7366 1553-7374 |
| language | English |
| publishDate | 2017-05-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj-art-3a6e1ba2df1a435299099f34e68cf1aa2025-08-20T02:31:59ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742017-05-01135e100637610.1371/journal.ppat.1006376Protein-protein interactions in the RPS4/RRS1 immune receptor complex.Sung Un HuhVolkan CevikPingtao DingZane DuxburyYan MaLaurence TomlinsonPanagiotis F SarrisJonathan D G JonesPlant 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.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006376&type=printable |
| spellingShingle | Sung Un Huh Volkan Cevik Pingtao Ding Zane Duxbury Yan Ma Laurence Tomlinson Panagiotis F Sarris Jonathan D G Jones Protein-protein interactions in the RPS4/RRS1 immune receptor complex. PLoS Pathogens |
| 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 |
| url | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1006376&type=printable |
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