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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...

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Autores principales: Wang, Xiaodan, Boevink, Petra, McLellan, Hazel, Armstrong, Miles, Bukharova, Tatyana, Qin, Zhiwei, Birch, Paul R.J.
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
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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.
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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
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