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LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2
In natural environments, plants often experience different stresses simultaneously, and adverse abiotic conditions can weaken the plant immune system. Interactome mapping revealed that the LOW SULPHUR UPREGULATED (LSU) proteins are hubs in an Arabidopsis protein interaction network that are targeted...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5441861/ https://www.ncbi.nlm.nih.gov/pubmed/28207043 http://dx.doi.org/10.1093/jxb/erw498 |
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author | Garcia-Molina, Antoni Altmann, Melina Alkofer, Angela Epple, Petra M. Dangl, Jeffery L. Falter-Braun, Pascal |
author_facet | Garcia-Molina, Antoni Altmann, Melina Alkofer, Angela Epple, Petra M. Dangl, Jeffery L. Falter-Braun, Pascal |
author_sort | Garcia-Molina, Antoni |
collection | PubMed |
description | In natural environments, plants often experience different stresses simultaneously, and adverse abiotic conditions can weaken the plant immune system. Interactome mapping revealed that the LOW SULPHUR UPREGULATED (LSU) proteins are hubs in an Arabidopsis protein interaction network that are targeted by virulence effectors from evolutionarily diverse pathogens. Here we show that LSU proteins are up-regulated in several abiotic and biotic stress conditions, such as nutrient depletion or salt stress, by both transcriptional and post-translational mechanisms. Interference with LSU expression prevents chloroplastic reactive oxygen species (ROS) production and proper stomatal closure during sulphur stress. We demonstrate that LSU1 interacts with the chloroplastic superoxide dismutase FSD2 and stimulates its enzymatic activity in vivo and in vitro. Pseudomonas syringae virulence effectors interfere with this interaction and preclude re-localization of LSU1 to chloroplasts. We demonstrate that reduced LSU levels cause a moderately enhanced disease susceptibility in plants exposed to abiotic stresses such as nutrient deficiency, high salinity, or heavy metal toxicity, whereas LSU1 overexpression confers significant disease resistance in several of these conditions. Our data suggest that the network hub LSU1 plays an important role in co-ordinating plant immune responses across a spectrum of abiotic stress conditions. |
format | Online Article Text |
id | pubmed-5441861 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-54418612017-05-30 LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 Garcia-Molina, Antoni Altmann, Melina Alkofer, Angela Epple, Petra M. Dangl, Jeffery L. Falter-Braun, Pascal J Exp Bot Research Paper In natural environments, plants often experience different stresses simultaneously, and adverse abiotic conditions can weaken the plant immune system. Interactome mapping revealed that the LOW SULPHUR UPREGULATED (LSU) proteins are hubs in an Arabidopsis protein interaction network that are targeted by virulence effectors from evolutionarily diverse pathogens. Here we show that LSU proteins are up-regulated in several abiotic and biotic stress conditions, such as nutrient depletion or salt stress, by both transcriptional and post-translational mechanisms. Interference with LSU expression prevents chloroplastic reactive oxygen species (ROS) production and proper stomatal closure during sulphur stress. We demonstrate that LSU1 interacts with the chloroplastic superoxide dismutase FSD2 and stimulates its enzymatic activity in vivo and in vitro. Pseudomonas syringae virulence effectors interfere with this interaction and preclude re-localization of LSU1 to chloroplasts. We demonstrate that reduced LSU levels cause a moderately enhanced disease susceptibility in plants exposed to abiotic stresses such as nutrient deficiency, high salinity, or heavy metal toxicity, whereas LSU1 overexpression confers significant disease resistance in several of these conditions. Our data suggest that the network hub LSU1 plays an important role in co-ordinating plant immune responses across a spectrum of abiotic stress conditions. Oxford University Press 2017-02-15 2017-02-16 /pmc/articles/PMC5441861/ /pubmed/28207043 http://dx.doi.org/10.1093/jxb/erw498 Text en © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. 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 reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Garcia-Molina, Antoni Altmann, Melina Alkofer, Angela Epple, Petra M. Dangl, Jeffery L. Falter-Braun, Pascal LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 |
title | LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 |
title_full | LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 |
title_fullStr | LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 |
title_full_unstemmed | LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 |
title_short | LSU network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase FSD2 |
title_sort | lsu network hubs integrate abiotic and biotic stress responses via interaction with the superoxide dismutase fsd2 |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5441861/ https://www.ncbi.nlm.nih.gov/pubmed/28207043 http://dx.doi.org/10.1093/jxb/erw498 |
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