Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity.
Identifieur interne : 001655 ( Main/Exploration ); précédent : 001654; suivant : 001656Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity.
Auteurs : Laurence S. Boutemy [Royaume-Uni] ; Stuart R F. King ; Joe Win ; Richard K. Hughes ; Thomas A. Clarke ; Tharin M A. Blumenschein ; Sophien Kamoun ; Mark J. BanfieldSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
Descripteurs français
- KwdFr :
- Facteurs de virulence (composition chimique), Facteurs de virulence (métabolisme), Maladies des plantes (microbiologie), Multimérisation de protéines (MeSH), Phytophthora infestans (composition chimique), Phytophthora infestans (pathogénicité), Pliage des protéines (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme), Spécificité d'espèce (MeSH), Structure quaternaire des protéines (MeSH), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH).
- MESH :
- composition chimique : Facteurs de virulence, Phytophthora infestans, Protéines fongiques.
- microbiologie : Maladies des plantes.
- métabolisme : Facteurs de virulence, Protéines fongiques.
- pathogénicité : Phytophthora infestans.
- Multimérisation de protéines, Pliage des protéines, Spécificité d'espèce, Structure quaternaire des protéines, Structure secondaire des protéines, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Fungal Proteins (chemistry), Fungal Proteins (metabolism), Phytophthora infestans (chemistry), Phytophthora infestans (pathogenicity), Plant Diseases (microbiology), Protein Folding (MeSH), Protein Multimerization (MeSH), Protein Structure, Quaternary (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Species Specificity (MeSH), Virulence Factors (chemistry), Virulence Factors (metabolism).
- MESH :
- chemical , chemistry : Fungal Proteins, Virulence Factors.
- chemical , metabolism : Fungal Proteins, Virulence Factors.
- chemistry : Phytophthora infestans.
- microbiology : Plant Diseases.
- pathogenicity : Phytophthora infestans.
- Protein Folding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Species Specificity.
Abstract
Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing <20% sequence identity in their effector domains, they display a conserved core α-helical fold. Bioinformatic analyses suggest that the core fold occurs in ∼44% of annotated Phytophthora RXLR effectors, both as a single domain and in tandem repeats of up to 11 units. Functionally important and polymorphic residues map to the surface of the structures, and PexRD2, but not AVR3a11, oligomerizes in planta. We conclude that the core α-helical fold enables functional adaptation of these fast evolving effectors through (i) insertion/deletions in loop regions between α-helices, (ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem domain duplications, and (v) oligomerization. We hypothesize that the molecular stability provided by this core fold, combined with considerable potential for plasticity, underlies the evolution of effectors that maintain their virulence activities while evading recognition by the plant immune system.
DOI: 10.1074/jbc.M111.262303
PubMed: 21813644
PubMed Central: PMC3195559
Affiliations:
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These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing <20% sequence identity in their effector domains, they display a conserved core α-helical fold. Bioinformatic analyses suggest that the core fold occurs in ∼44% of annotated Phytophthora RXLR effectors, both as a single domain and in tandem repeats of up to 11 units. Functionally important and polymorphic residues map to the surface of the structures, and PexRD2, but not AVR3a11, oligomerizes in planta. We conclude that the core α-helical fold enables functional adaptation of these fast evolving effectors through (i) insertion/deletions in loop regions between α-helices, (ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem domain duplications, and (v) oligomerization. We hypothesize that the molecular stability provided by this core fold, combined with considerable potential for plasticity, underlies the evolution of effectors that maintain their virulence activities while evading recognition by the plant immune system.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21813644</PMID><DateCompleted><Year>2011</Year><Month>12</Month><Day>12</Day></DateCompleted><DateRevised><Year>2019</Year><Month>10</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>286</Volume><Issue>41</Issue><PubDate><Year>2011</Year><Month>Oct</Month><Day>14</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity.</ArticleTitle><Pagination><MedlinePgn>35834-42</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M111.262303</ELocationID><Abstract><AbstractText>Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing <20% sequence identity in their effector domains, they display a conserved core α-helical fold. Bioinformatic analyses suggest that the core fold occurs in ∼44% of annotated Phytophthora RXLR effectors, both as a single domain and in tandem repeats of up to 11 units. Functionally important and polymorphic residues map to the surface of the structures, and PexRD2, but not AVR3a11, oligomerizes in planta. We conclude that the core α-helical fold enables functional adaptation of these fast evolving effectors through (i) insertion/deletions in loop regions between α-helices, (ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem domain duplications, and (v) oligomerization. We hypothesize that the molecular stability provided by this core fold, combined with considerable potential for plasticity, underlies the evolution of effectors that maintain their virulence activities while evading recognition by the plant immune system.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Boutemy</LastName><ForeName>Laurence S</ForeName><Initials>LS</Initials><AffiliationInfo><Affiliation>Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>King</LastName><ForeName>Stuart R F</ForeName><Initials>SR</Initials></Author><Author ValidYN="Y"><LastName>Win</LastName><ForeName>Joe</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Hughes</LastName><ForeName>Richard K</ForeName><Initials>RK</Initials></Author><Author ValidYN="Y"><LastName>Clarke</LastName><ForeName>Thomas 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Banfield</name><name sortKey="Blumenschein, Tharin M A" sort="Blumenschein, Tharin M A" uniqKey="Blumenschein T" first="Tharin M A" last="Blumenschein">Tharin M A. Blumenschein</name><name sortKey="Clarke, Thomas A" sort="Clarke, Thomas A" uniqKey="Clarke T" first="Thomas A" last="Clarke">Thomas A. Clarke</name><name sortKey="Hughes, Richard K" sort="Hughes, Richard K" uniqKey="Hughes R" first="Richard K" last="Hughes">Richard K. Hughes</name><name sortKey="Kamoun, Sophien" sort="Kamoun, Sophien" uniqKey="Kamoun S" first="Sophien" last="Kamoun">Sophien Kamoun</name><name sortKey="King, Stuart R F" sort="King, Stuart R F" uniqKey="King S" first="Stuart R F" last="King">Stuart R F. King</name><name sortKey="Win, Joe" sort="Win, Joe" uniqKey="Win J" first="Joe" last="Win">Joe Win</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Boutemy, Laurence S" sort="Boutemy, Laurence S" uniqKey="Boutemy L" first="Laurence S" last="Boutemy">Laurence S. 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