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The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis

Ralstonia solanacearum, one of the most destructive plant bacterial pathogens, delivers an array of effector proteins via its type III secretion system for pathogenesis. However, the biochemical functions of most of these proteins remain unclear. RipN is a type III effector with unknown function(s)...

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Autores principales: Sun, Yunhao, Li, Pai, Shen, Dong, Wei, Qiaoling, He, Jianguo, Lu, Yongjun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637912/
https://www.ncbi.nlm.nih.gov/pubmed/30499216
http://dx.doi.org/10.1111/mpp.12773
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author Sun, Yunhao
Li, Pai
Shen, Dong
Wei, Qiaoling
He, Jianguo
Lu, Yongjun
author_facet Sun, Yunhao
Li, Pai
Shen, Dong
Wei, Qiaoling
He, Jianguo
Lu, Yongjun
author_sort Sun, Yunhao
collection PubMed
description Ralstonia solanacearum, one of the most destructive plant bacterial pathogens, delivers an array of effector proteins via its type III secretion system for pathogenesis. However, the biochemical functions of most of these proteins remain unclear. RipN is a type III effector with unknown function(s) from the pathogen R. solanacearum. Here, we demonstrate that RipN is a conserved type III effector found within the R. solanacearum species complex that contains a putative Nudix hydrolase domain and has ADP‐ribose/NADH pyrophosphorylase activity in vitro. Further analysis shows that RipN localizes to the endoplasmic reticulum (ER) and nucleus in Nicotiana tabacum leaf cells and Arabidopsis protoplasts, and truncation of the C‐terminus of RipN results in a loss of nuclear and ER targeting. Furthermore, the expression of RipN in Arabidopsis suppresses callose deposition and the transcription of pathogen‐associated molecular pattern (PAMP)‐triggered immunity (PTI) marker genes under flg22 treatment, and promotes bacterial growth in planta. In addition, the expression of RipN in plant cells alters NADH/NAD(+), but not GSH/GSSG, ratios, and its Nudix hydrolase activity is indispensable for such biochemical function. These results suggest that RipN acts as a Nudix hydrolase, alters the NADH/NAD(+) ratio of the plant and contributes to R. solanacearum virulence by suppression of PTI of the host.
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spelling pubmed-66379122019-09-16 The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis Sun, Yunhao Li, Pai Shen, Dong Wei, Qiaoling He, Jianguo Lu, Yongjun Mol Plant Pathol Original Articles Ralstonia solanacearum, one of the most destructive plant bacterial pathogens, delivers an array of effector proteins via its type III secretion system for pathogenesis. However, the biochemical functions of most of these proteins remain unclear. RipN is a type III effector with unknown function(s) from the pathogen R. solanacearum. Here, we demonstrate that RipN is a conserved type III effector found within the R. solanacearum species complex that contains a putative Nudix hydrolase domain and has ADP‐ribose/NADH pyrophosphorylase activity in vitro. Further analysis shows that RipN localizes to the endoplasmic reticulum (ER) and nucleus in Nicotiana tabacum leaf cells and Arabidopsis protoplasts, and truncation of the C‐terminus of RipN results in a loss of nuclear and ER targeting. Furthermore, the expression of RipN in Arabidopsis suppresses callose deposition and the transcription of pathogen‐associated molecular pattern (PAMP)‐triggered immunity (PTI) marker genes under flg22 treatment, and promotes bacterial growth in planta. In addition, the expression of RipN in plant cells alters NADH/NAD(+), but not GSH/GSSG, ratios, and its Nudix hydrolase activity is indispensable for such biochemical function. These results suggest that RipN acts as a Nudix hydrolase, alters the NADH/NAD(+) ratio of the plant and contributes to R. solanacearum virulence by suppression of PTI of the host. John Wiley and Sons Inc. 2019-02-18 /pmc/articles/PMC6637912/ /pubmed/30499216 http://dx.doi.org/10.1111/mpp.12773 Text en © 2018 The Authors. Molecular Plant Pathology Published by BSPP and John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Sun, Yunhao
Li, Pai
Shen, Dong
Wei, Qiaoling
He, Jianguo
Lu, Yongjun
The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis
title The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis
title_full The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis
title_fullStr The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis
title_full_unstemmed The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis
title_short The Ralstonia solanacearum effector RipN suppresses plant PAMP‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the NADH/NAD(+) ratio in Arabidopsis
title_sort ralstonia solanacearum effector ripn suppresses plant pamp‐triggered immunity, localizes to the endoplasmic reticulum and nucleus, and alters the nadh/nad(+) ratio in arabidopsis
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6637912/
https://www.ncbi.nlm.nih.gov/pubmed/30499216
http://dx.doi.org/10.1111/mpp.12773
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