Cargando…
A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease()
Plant pathogens deliver effector proteins that alter host processes to create an environment conducive to colonization. Attention has focused on identifying the targets of effectors and how their manipulation facilitates disease. RXLR effector Pi04089 from the potato blight pathogen Phytophthora inf...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4560694/ https://www.ncbi.nlm.nih.gov/pubmed/25936676 http://dx.doi.org/10.1016/j.molp.2015.04.012 |
_version_ | 1782388948315668480 |
---|---|
author | Wang, Xiaodan Boevink, Petra McLellan, Hazel Armstrong, Miles Bukharova, Tatyana Qin, Zhiwei Birch, Paul R.J. |
author_facet | Wang, Xiaodan Boevink, Petra McLellan, Hazel Armstrong, Miles Bukharova, Tatyana Qin, Zhiwei Birch, Paul R.J. |
author_sort | Wang, Xiaodan |
collection | PubMed |
description | Plant pathogens deliver effector proteins that alter host processes to create an environment conducive to colonization. Attention has focused on identifying the targets of effectors and how their manipulation facilitates disease. RXLR effector Pi04089 from the potato blight pathogen Phytophthora infestans accumulates in the host nucleus and enhances colonization when transiently expressed in planta. Its nuclear localization is required for enhanced P. infestans colonization. Pi04089 interacts in yeast and in planta with a putative potato K-homology (KH) RNA-binding protein, StKRBP1. Co-localization of Pi04089 and StKRBP1, and bimolecular fluorescence complementation between them, indicate they associate at nuclear speckles. StKRBP1 protein levels increased when it was co-expressed with Pi04089. Indeed, such accumulation of StKRBP1 was observed also on the first day of leaf colonization by the pathogen. Remarkably, overexpression of StKRBP1 significantly enhances P. infestans infection. Mutation of the nucleotide-binding motif GxxG to GDDG in all three KH domains of StKRBP1 abolishes its interaction with Pi04089, its localization to nuclear speckles, and its increased accumulation when co-expressed with the effector. Moreover, the mutant StKRBP1 protein no longer enhances leaf colonization by P. infestans, implying that nucleotide binding is likely required for this activity. We thus argue that StKRBP1 can be regarded as a susceptibility factor, as its activity is beneficial to the pathogen. |
format | Online Article Text |
id | pubmed-4560694 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-45606942015-10-26 A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() Wang, Xiaodan Boevink, Petra McLellan, Hazel Armstrong, Miles Bukharova, Tatyana Qin, Zhiwei Birch, Paul R.J. Mol Plant Research Article Plant pathogens deliver effector proteins that alter host processes to create an environment conducive to colonization. Attention has focused on identifying the targets of effectors and how their manipulation facilitates disease. RXLR effector Pi04089 from the potato blight pathogen Phytophthora infestans accumulates in the host nucleus and enhances colonization when transiently expressed in planta. Its nuclear localization is required for enhanced P. infestans colonization. Pi04089 interacts in yeast and in planta with a putative potato K-homology (KH) RNA-binding protein, StKRBP1. Co-localization of Pi04089 and StKRBP1, and bimolecular fluorescence complementation between them, indicate they associate at nuclear speckles. StKRBP1 protein levels increased when it was co-expressed with Pi04089. Indeed, such accumulation of StKRBP1 was observed also on the first day of leaf colonization by the pathogen. Remarkably, overexpression of StKRBP1 significantly enhances P. infestans infection. Mutation of the nucleotide-binding motif GxxG to GDDG in all three KH domains of StKRBP1 abolishes its interaction with Pi04089, its localization to nuclear speckles, and its increased accumulation when co-expressed with the effector. Moreover, the mutant StKRBP1 protein no longer enhances leaf colonization by P. infestans, implying that nucleotide binding is likely required for this activity. We thus argue that StKRBP1 can be regarded as a susceptibility factor, as its activity is beneficial to the pathogen. Oxford University Press 2015-09-07 /pmc/articles/PMC4560694/ /pubmed/25936676 http://dx.doi.org/10.1016/j.molp.2015.04.012 Text en © 2015 The Author http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Article Wang, Xiaodan Boevink, Petra McLellan, Hazel Armstrong, Miles Bukharova, Tatyana Qin, Zhiwei Birch, Paul R.J. A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() |
title | A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() |
title_full | A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() |
title_fullStr | A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() |
title_full_unstemmed | A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() |
title_short | A Host KH RNA-Binding Protein Is a Susceptibility Factor Targeted by an RXLR Effector to Promote Late Blight Disease() |
title_sort | host kh rna-binding protein is a susceptibility factor targeted by an rxlr effector to promote late blight disease() |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4560694/ https://www.ncbi.nlm.nih.gov/pubmed/25936676 http://dx.doi.org/10.1016/j.molp.2015.04.012 |
work_keys_str_mv | AT wangxiaodan ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT boevinkpetra ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT mclellanhazel ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT armstrongmiles ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT bukharovatatyana ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT qinzhiwei ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT birchpaulrj ahostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT wangxiaodan hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT boevinkpetra hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT mclellanhazel hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT armstrongmiles hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT bukharovatatyana hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT qinzhiwei hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease AT birchpaulrj hostkhrnabindingproteinisasusceptibilityfactortargetedbyanrxlreffectortopromotelateblightdisease |