Structural analysis of Phytophthora suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.
Identifieur interne : 000515 ( Main/Corpus ); précédent : 000514; suivant : 000516Structural analysis of Phytophthora suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.
Auteurs : Jinqiu He ; Wenwu Ye ; Du Seok Choi ; Baixing Wu ; Yi Zhai ; Baodian Guo ; Shuyi Duan ; Yuanchao Wang ; Jianhua Gan ; Wenbo Ma ; Jinbiao MaSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2019.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Bacterial Proteins.
- chemistry : Phytophthora.
- genetics : Amino Acid Motifs, Bacterial Proteins, Phytophthora, Tandem Repeat Sequences.
- microbiology : Plant Diseases.
- pathogenicity : Phytophthora.
- physiology : Amino Acid Motifs.
- Models, Molecular.
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
Links to Exploration step
pubmed:30926664Le document en format XML
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<term>Bacterial Proteins (genetics)</term>
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<term>Bacterial Proteins</term>
<term>Phytophthora</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>
</TEI>
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<ArticleTitle>Structural analysis of <i>Phytophthora</i>
suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.</ArticleTitle>
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<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>
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<Initials>J</Initials>
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<Author ValidYN="Y"><LastName>Ye</LastName>
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<AffiliationInfo><Affiliation>Department of Plant Pathology, Nanjing Agriculture University, 210095 Nanjing, China.</Affiliation>
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<Keyword MajorTopicYN="Y">protein diversification</Keyword>
<Keyword MajorTopicYN="Y">tandem repeats</Keyword>
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