Serveur d'exploration Phytophthora

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Structural analysis of Phytophthora suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.

Identifieur interne : 000381 ( Main/Exploration ); précédent : 000380; suivant : 000382

Structural analysis of Phytophthora suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.

Auteurs : Jinqiu He [République populaire de Chine] ; Wenwu Ye [République populaire de Chine] ; Du Seok Choi [États-Unis] ; Baixing Wu [République populaire de Chine] ; Yi Zhai [États-Unis] ; Baodian Guo [République populaire de Chine] ; Shuyi Duan [République populaire de Chine] ; Yuanchao Wang [République populaire de Chine] ; Jianhua Gan [République populaire de Chine] ; Wenbo Ma [États-Unis] ; Jinbiao Ma [États-Unis]

Source :

RBID : pubmed:30926664

Descripteurs français

English descriptors

Abstract

Phytophthora are eukaryotic pathogens that cause enormous losses in agriculture and forestry. Each Phytophthora species encodes hundreds of effector proteins that collectively have essential roles in manipulating host cellular processes and facilitating disease development. Here we report the crystal structure of the effector Phytophthora suppressor of RNA silencing 2 (PSR2). PSR2 produced by the soybean pathogen Phytophthora sojae (PsPSR2) consists of seven tandem repeat units, including one W-Y motif and six L-W-Y motifs. Each L-W-Y motif forms a highly conserved fold consisting of five α-helices. Adjacent units are connected through stable, directional linkages between an internal loop at the C terminus of one unit and a hydrophobic pocket at the N terminus of the following unit. This unique concatenation results in an overall stick-like structure of PsPSR2. Genome-wide analyses reveal 293 effectors from five Phytophthora species that have the PsPSR2-like arrangement, that is, containing a W-Y motif as the "start" unit, various numbers of L-W-Y motifs as the "middle" units, and a degenerate L-W-Y as the "end" unit. Residues involved in the interunit interactions show significant conservation, suggesting that these effectors also use the conserved concatenation mechanism. Furthermore, functional analysis demonstrates differential contributions of individual units to the virulence activity of PsPSR2. These findings suggest that the L-W-Y fold is a basic structural and functional module that may serve as a "building block" to accelerate effector evolution in Phytophthora.

DOI: 10.1073/pnas.1819481116
PubMed: 30926664
PubMed Central: PMC6475376


Affiliations:


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Le document en format XML

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<title level="j">Proceedings of the National Academy of Sciences of the United States of America</title>
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<term>Amino Acid Motifs (genetics)</term>
<term>Amino Acid Motifs (physiology)</term>
<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (genetics)</term>
<term>Models, Molecular (MeSH)</term>
<term>Phytophthora (chemistry)</term>
<term>Phytophthora (genetics)</term>
<term>Phytophthora (pathogenicity)</term>
<term>Plant Diseases (microbiology)</term>
<term>Tandem Repeat Sequences (genetics)</term>
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<term>Maladies des plantes (microbiologie)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Motifs d'acides aminés (génétique)</term>
<term>Motifs d'acides aminés (physiologie)</term>
<term>Phytophthora (composition chimique)</term>
<term>Phytophthora (génétique)</term>
<term>Phytophthora (pathogénicité)</term>
<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (génétique)</term>
<term>Séquences répétées en tandem (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Bacterial Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en">
<term>Phytophthora</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>Phytophthora</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Amino Acid Motifs</term>
<term>Bacterial Proteins</term>
<term>Phytophthora</term>
<term>Tandem Repeat Sequences</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Motifs d'acides aminés</term>
<term>Phytophthora</term>
<term>Protéines bactériennes</term>
<term>Séquences répétées en tandem</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr">
<term>Maladies des plantes</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en">
<term>Plant Diseases</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en">
<term>Phytophthora</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr">
<term>Phytophthora</term>
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<term>Motifs d'acides aminés</term>
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</keywords>
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<term>Models, Molecular</term>
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<front>
<div type="abstract" xml:lang="en">
<i>Phytophthora</i>
are eukaryotic pathogens that cause enormous losses in agriculture and forestry. Each
<i>Phytophthora</i>
species encodes hundreds of effector proteins that collectively have essential roles in manipulating host cellular processes and facilitating disease development. Here we report the crystal structure of the effector
<i>Phytophthora</i>
suppressor of RNA silencing 2 (PSR2). PSR2 produced by the soybean pathogen
<i>Phytophthora sojae</i>
(
<i>Ps</i>
PSR2) consists of seven tandem repeat units, including one W-Y motif and six L-W-Y motifs. Each L-W-Y motif forms a highly conserved fold consisting of five α-helices. Adjacent units are connected through stable, directional linkages between an internal loop at the C terminus of one unit and a hydrophobic pocket at the N terminus of the following unit. This unique concatenation results in an overall stick-like structure of
<i>Ps</i>
PSR2. Genome-wide analyses reveal 293 effectors from five
<i>Phytophthora</i>
species that have the
<i>Ps</i>
PSR2-like arrangement, that is, containing a W-Y motif as the "start" unit, various numbers of L-W-Y motifs as the "middle" units, and a degenerate L-W-Y as the "end" unit. Residues involved in the interunit interactions show significant conservation, suggesting that these effectors also use the conserved concatenation mechanism. Furthermore, functional analysis demonstrates differential contributions of individual units to the virulence activity of
<i>Ps</i>
PSR2. These findings suggest that the L-W-Y fold is a basic structural and functional module that may serve as a "building block" to accelerate effector evolution in
<i>Phytophthora</i>
.</div>
</front>
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<Article PubModel="Print-Electronic">
<Journal>
<ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>116</Volume>
<Issue>16</Issue>
<PubDate>
<Year>2019</Year>
<Month>04</Month>
<Day>16</Day>
</PubDate>
</JournalIssue>
<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation>
</Journal>
<ArticleTitle>Structural analysis of
<i>Phytophthora</i>
suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.</ArticleTitle>
<Pagination>
<MedlinePgn>8054-8059</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1819481116</ELocationID>
<Abstract>
<AbstractText>
<i>Phytophthora</i>
are eukaryotic pathogens that cause enormous losses in agriculture and forestry. Each
<i>Phytophthora</i>
species encodes hundreds of effector proteins that collectively have essential roles in manipulating host cellular processes and facilitating disease development. Here we report the crystal structure of the effector
<i>Phytophthora</i>
suppressor of RNA silencing 2 (PSR2). PSR2 produced by the soybean pathogen
<i>Phytophthora sojae</i>
(
<i>Ps</i>
PSR2) consists of seven tandem repeat units, including one W-Y motif and six L-W-Y motifs. Each L-W-Y motif forms a highly conserved fold consisting of five α-helices. Adjacent units are connected through stable, directional linkages between an internal loop at the C terminus of one unit and a hydrophobic pocket at the N terminus of the following unit. This unique concatenation results in an overall stick-like structure of
<i>Ps</i>
PSR2. Genome-wide analyses reveal 293 effectors from five
<i>Phytophthora</i>
species that have the
<i>Ps</i>
PSR2-like arrangement, that is, containing a W-Y motif as the "start" unit, various numbers of L-W-Y motifs as the "middle" units, and a degenerate L-W-Y as the "end" unit. Residues involved in the interunit interactions show significant conservation, suggesting that these effectors also use the conserved concatenation mechanism. Furthermore, functional analysis demonstrates differential contributions of individual units to the virulence activity of
<i>Ps</i>
PSR2. These findings suggest that the L-W-Y fold is a basic structural and functional module that may serve as a "building block" to accelerate effector evolution in
<i>Phytophthora</i>
.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>He</LastName>
<ForeName>Jinqiu</ForeName>
<Initials>J</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Genetic Engineering, Ministry of Education Key Laboratory of Biodiversity Sciences and Ecological Engineering, Institute of Plant Biology, School of Life Sciences, Fudan University, 200438 Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Ye</LastName>
<ForeName>Wenwu</ForeName>
<Initials>W</Initials>
<Identifier Source="ORCID">0000-0001-7347-8935</Identifier>
<AffiliationInfo>
<Affiliation>Department of Plant Pathology, Nanjing Agriculture University, 210095 Nanjing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Choi</LastName>
<ForeName>Du Seok</ForeName>
<Initials>DS</Initials>
<AffiliationInfo>
<Affiliation>Department of Microbiology and Plant Pathology, University of California, Riverside, CA 92521.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Center for Plant Cell Biology, University of California, Riverside, CA 92521.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Wu</LastName>
<ForeName>Baixing</ForeName>
<Initials>B</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Genetic Engineering, Ministry of Education Key Laboratory of Biodiversity Sciences and Ecological Engineering, Institute of Plant Biology, School of Life Sciences, Fudan University, 200438 Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Zhai</LastName>
<ForeName>Yi</ForeName>
<Initials>Y</Initials>
<AffiliationInfo>
<Affiliation>Department of Microbiology and Plant Pathology, University of California, Riverside, CA 92521.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Center for Plant Cell Biology, University of California, Riverside, CA 92521.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Guo</LastName>
<ForeName>Baodian</ForeName>
<Initials>B</Initials>
<AffiliationInfo>
<Affiliation>Department of Plant Pathology, Nanjing Agriculture University, 210095 Nanjing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Duan</LastName>
<ForeName>Shuyi</ForeName>
<Initials>S</Initials>
<AffiliationInfo>
<Affiliation>Department of Plant Pathology, Nanjing Agriculture University, 210095 Nanjing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Wang</LastName>
<ForeName>Yuanchao</ForeName>
<Initials>Y</Initials>
<AffiliationInfo>
<Affiliation>Department of Plant Pathology, Nanjing Agriculture University, 210095 Nanjing, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Gan</LastName>
<ForeName>Jianhua</ForeName>
<Initials>J</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Genetic Engineering, Department of Physiology and Biophysics, School of Life Sciences, Fudan University, 200438 Shanghai, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Ma</LastName>
<ForeName>Wenbo</ForeName>
<Initials>W</Initials>
<AffiliationInfo>
<Affiliation>Department of Microbiology and Plant Pathology, University of California, Riverside, CA 92521; wenbo.ma@ucr.edu majb@fudan.edu.cn.</Affiliation>
</AffiliationInfo>
<AffiliationInfo>
<Affiliation>Center for Plant Cell Biology, University of California, Riverside, CA 92521.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Ma</LastName>
<ForeName>Jinbiao</ForeName>
<Initials>J</Initials>
<Identifier Source="ORCID">0000-0002-0232-1786</Identifier>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Genetic Engineering, Ministry of Education Key Laboratory of Biodiversity Sciences and Ecological Engineering, Institute of Plant Biology, School of Life Sciences, Fudan University, 200438 Shanghai, China; wenbo.ma@ucr.edu majb@fudan.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y">
<DataBank>
<DataBankName>PDB</DataBankName>
<AccessionNumberList>
<AccessionNumber>5GNC</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2019</Year>
<Month>03</Month>
<Day>29</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>United States</Country>
<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
<NlmUniqueID>7505876</NlmUniqueID>
<ISSNLinking>0027-8424</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D020080" MajorTopicYN="N">Tandem Repeat Sequences</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="Y">Phytophthora disease</Keyword>
<Keyword MajorTopicYN="Y">effector evolution</Keyword>
<Keyword MajorTopicYN="Y">microbial pathogenesis</Keyword>
<Keyword MajorTopicYN="Y">protein diversification</Keyword>
<Keyword MajorTopicYN="Y">tandem repeats</Keyword>
</KeywordList>
<CoiStatement>The authors declare no conflict of interest.</CoiStatement>
</MedlineCitation>
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