Serveur d'exploration Phytophthora

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The WY domain in the Phytophthora effector PSR1 is required for infection and RNA silencing suppression activity.

Identifieur interne : 000363 ( Main/Exploration ); précédent : 000362; suivant : 000364

The WY domain in the Phytophthora effector PSR1 is required for infection and RNA silencing suppression activity.

Auteurs : Peng Zhang [République populaire de Chine] ; Yijuan Jia [République populaire de Chine] ; Jinxia Shi [République populaire de Chine] ; Chen Chen [République populaire de Chine] ; Wenwu Ye [République populaire de Chine] ; Yuanchao Wang [République populaire de Chine] ; Wenbo Ma [États-Unis] ; Yongli Qiao [République populaire de Chine]

Source :

RBID : pubmed:30963588

Descripteurs français

English descriptors

Abstract

Phytophthora pathogens manipulate host innate immunity by secreting numerous RxLR effectors, thereby facilitating pathogen colonization. Predicted single and tandem repeats of WY domains are the most prominent C-terminal motifs conserved across the Phytophthora RxLR superfamily. However, the functions of individual WY domains in effectors remain poorly understood. The Phytophthora sojae effector PSR1 promotes infection by suppressing small RNA biogenesis in plant hosts. We identified one single WY domain following the RxLR motif in PSR1. This domain was required for RNA silencing suppression activity and infection in Nicotiana benthamiana, Arabidopsis and soybean. Mutations of the conserved residues in the WY domain did not affect the subcellular localization of PSR1 but abolished its effect on plant development and resistance to viral and Phytophthora pathogens. This is at least in part due to decreased protein stability of the PSR1 mutants in planta. The identification of the WY domain in PSR1 allows predicts that a family of PSR1-like effectors also possess RNA silencing suppression activity. Mutation of the conserved residues in two members of this family, PpPSR1L from P. parasitica and PcPSR1L from P. capsici, perturbed their biological functions, indicating that the WY domain is critical in Phytophthora PSR1 and PSR1-like effectors.

DOI: 10.1111/nph.15836
PubMed: 30963588


Affiliations:


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<div type="abstract" xml:lang="en">Phytophthora pathogens manipulate host innate immunity by secreting numerous RxLR effectors, thereby facilitating pathogen colonization. Predicted single and tandem repeats of WY domains are the most prominent C-terminal motifs conserved across the Phytophthora RxLR superfamily. However, the functions of individual WY domains in effectors remain poorly understood. The Phytophthora sojae effector PSR1 promotes infection by suppressing small RNA biogenesis in plant hosts. We identified one single WY domain following the RxLR motif in PSR1. This domain was required for RNA silencing suppression activity and infection in Nicotiana benthamiana, Arabidopsis and soybean. Mutations of the conserved residues in the WY domain did not affect the subcellular localization of PSR1 but abolished its effect on plant development and resistance to viral and Phytophthora pathogens. This is at least in part due to decreased protein stability of the PSR1 mutants in planta. The identification of the WY domain in PSR1 allows predicts that a family of PSR1-like effectors also possess RNA silencing suppression activity. Mutation of the conserved residues in two members of this family, PpPSR1L from P. parasitica and PcPSR1L from P. capsici, perturbed their biological functions, indicating that the WY domain is critical in Phytophthora PSR1 and PSR1-like effectors.</div>
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<Initials>Y</Initials>
<Identifier Source="ORCID">0000-0001-9178-5293</Identifier>
<AffiliationInfo>
<Affiliation>Shanghai Key Laboratory of Plant Molecular Sciences, College of Life Sciences, Shanghai Normal University, Shanghai, 200234, China.</Affiliation>
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<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<ArticleDate DateType="Electronic">
<Year>2019</Year>
<Month>06</Month>
<Day>18</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>England</Country>
<MedlineTA>New Phytol</MedlineTA>
<NlmUniqueID>9882884</NlmUniqueID>
<ISSNLinking>0028-646X</ISSNLinking>
</MedlineJournalInfo>
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<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011506">Proteins</NameOfSubstance>
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<DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName>
<QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName>
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<DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
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<DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName>
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<DescriptorName UI="D018517" MajorTopicYN="N">Plant Roots</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
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<DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
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<DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
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<DescriptorName UI="D013025" MajorTopicYN="N">Soybeans</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
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<Keyword MajorTopicYN="Y">PSR1</Keyword>
<Keyword MajorTopicYN="Y">Phytophthora pathogenesis</Keyword>
<Keyword MajorTopicYN="Y">RNA silencing</Keyword>
<Keyword MajorTopicYN="Y">RxLR effector</Keyword>
<Keyword MajorTopicYN="Y">WY domains</Keyword>
<Keyword MajorTopicYN="Y">host-pathogen interaction</Keyword>
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<Year>2019</Year>
<Month>02</Month>
<Day>20</Day>
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<PubMedPubDate PubStatus="accepted">
<Year>2019</Year>
<Month>03</Month>
<Day>29</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed">
<Year>2019</Year>
<Month>4</Month>
<Day>10</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline">
<Year>2020</Year>
<Month>3</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="entrez">
<Year>2019</Year>
<Month>4</Month>
<Day>10</Day>
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<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">30963588</ArticleId>
<ArticleId IdType="doi">10.1111/nph.15836</ArticleId>
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<list>
<country>
<li>République populaire de Chine</li>
<li>États-Unis</li>
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<name sortKey="Zhang, Peng" sort="Zhang, Peng" uniqKey="Zhang P" first="Peng" last="Zhang">Peng Zhang</name>
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<name sortKey="Chen, Chen" sort="Chen, Chen" uniqKey="Chen C" first="Chen" last="Chen">Chen Chen</name>
<name sortKey="Chen, Chen" sort="Chen, Chen" uniqKey="Chen C" first="Chen" last="Chen">Chen Chen</name>
<name sortKey="Jia, Yijuan" sort="Jia, Yijuan" uniqKey="Jia Y" first="Yijuan" last="Jia">Yijuan Jia</name>
<name sortKey="Qiao, Yongli" sort="Qiao, Yongli" uniqKey="Qiao Y" first="Yongli" last="Qiao">Yongli Qiao</name>
<name sortKey="Shi, Jinxia" sort="Shi, Jinxia" uniqKey="Shi J" first="Jinxia" last="Shi">Jinxia Shi</name>
<name sortKey="Wang, Yuanchao" sort="Wang, Yuanchao" uniqKey="Wang Y" first="Yuanchao" last="Wang">Yuanchao Wang</name>
<name sortKey="Ye, Wenwu" sort="Ye, Wenwu" uniqKey="Ye W" first="Wenwu" last="Ye">Wenwu Ye</name>
<name sortKey="Zhang, Peng" sort="Zhang, Peng" uniqKey="Zhang P" first="Peng" last="Zhang">Peng Zhang</name>
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<name sortKey="Ma, Wenbo" sort="Ma, Wenbo" uniqKey="Ma W" first="Wenbo" last="Ma">Wenbo Ma</name>
</country>
</tree>
</affiliations>
</record>

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