PhytophthoraEffectorV1, Main, Exploration, bibRecord, 000252

Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity.

Identifieur interne : 000252 ( Main/Exploration ); précédent : 000251; suivant : 000253

Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity.

Auteurs : Takashi Yaeno [Japon] ; Hua Li ; Angela Chaparro-Garcia ; Sebastian Schornack ; Seizo Koshiba ; Satoru Watanabe ; Takanori Kigawa ; Sophien Kamoun ; Ken Shirasu

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2011.

RBID : pubmed:21821794

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Magnetic Resonance Spectroscopy (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Phosphatidylinositol Phosphates (metabolism), Phytophthora infestans (pathogenicity), Plant Immunity (MeSH), Protein Folding (MeSH), Protein Structure, Tertiary (MeSH), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Ubiquitin-Protein Ligases (physiology), Virulence Factors (chemistry), Virulence Factors (metabolism), Virulence Factors (physiology).
MESH :
- chemical , chemistry : Virulence Factors.
- chemical , metabolism : Phosphatidylinositol Phosphates, Virulence Factors.
- pathogenicity : Phytophthora infestans.
- chemical , physiology : Ubiquitin-Protein Ligases, Virulence Factors.
- Amino Acid Motifs, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Plant Immunity, Protein Folding, Protein Structure, Tertiary, Sequence Alignment, Sequence Homology, Amino Acid.

Abstract

The oomycete pathogen Phytophthora infestans causes potato late blight, one of the most economically damaging plant diseases worldwide. P. infestans produces AVR3a, an essential modular virulence effector with an N-terminal RXLR domain that is required for host-cell entry. In host cells, AVR3a stabilizes and inhibits the function of the E3 ubiquitin ligase CMPG1, a key factor in host immune responses including cell death triggered by the pathogen-derived elicitor protein INF1 elicitin. To elucidate the molecular basis of AVR3a effector function, we determined the structure of Phytophthora capsici AVR3a4, a close homolog of P. infestans AVR3a. Our structural and functional analyses reveal that the effector domain of AVR3a contains a conserved, positively charged patch and that this region, rather than the RXLR domain, is required for binding to phosphatidylinositol monophosphates (PIPs) in vitro. Mutations affecting PIP binding do not abolish AVR3a recognition by the resistance protein R3a but reduce its ability to suppress INF1-triggered cell death in planta. Similarly, stabilization of CMPG1 in planta is diminished by these mutations. The steady-state levels of non-PIP-binding mutant proteins in planta are reduced greatly, although these proteins are stable in vitro. Furthermore, overexpression of a phosphatidylinositol phosphate 5-kinase results in reduction of AVR3a levels in planta. Our results suggest that the PIP-binding ability of the AVR3a effector domain is essential for its accumulation inside host cells to suppress CMPG1-dependent immunity.

DOI: 10.1073/pnas.1106002108
PubMed: 21821794
PubMed Central: PMC3167543

Affiliations:

Japon

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000244
to stream Main, to step Curation: 000244

Le document en format XML

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<term>Molecular Sequence Data (MeSH)</term>
<term>Phosphatidylinositol Phosphates (metabolism)</term>
<term>Phytophthora infestans (pathogenicity)</term>
<term>Plant Immunity (MeSH)</term>
<term>Protein Folding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
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<term>Facteurs de virulence ()</term>
<term>Facteurs de virulence (métabolisme)</term>
<term>Facteurs de virulence (physiologie)</term>
<term>Immunité des plantes (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Motifs d'acides aminés (MeSH)</term>
<term>Phosphates phosphatidylinositol (métabolisme)</term>
<term>Phytophthora infestans (pathogénicité)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Spectroscopie par résonance magnétique (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Ubiquitin-protein ligases (physiologie)</term>
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<term>Virulence Factors</term>
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<term>Phosphates phosphatidylinositol</term>
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<term>Modèles moléculaires</term>
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<term>Pliage des protéines</term>
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<front><div type="abstract" xml:lang="en">The oomycete pathogen Phytophthora infestans causes potato late blight, one of the most economically damaging plant diseases worldwide. P. infestans produces AVR3a, an essential modular virulence effector with an N-terminal RXLR domain that is required for host-cell entry. In host cells, AVR3a stabilizes and inhibits the function of the E3 ubiquitin ligase CMPG1, a key factor in host immune responses including cell death triggered by the pathogen-derived elicitor protein INF1 elicitin. To elucidate the molecular basis of AVR3a effector function, we determined the structure of Phytophthora capsici AVR3a4, a close homolog of P. infestans AVR3a. Our structural and functional analyses reveal that the effector domain of AVR3a contains a conserved, positively charged patch and that this region, rather than the RXLR domain, is required for binding to phosphatidylinositol monophosphates (PIPs) in vitro. Mutations affecting PIP binding do not abolish AVR3a recognition by the resistance protein R3a but reduce its ability to suppress INF1-triggered cell death in planta. Similarly, stabilization of CMPG1 in planta is diminished by these mutations. The steady-state levels of non-PIP-binding mutant proteins in planta are reduced greatly, although these proteins are stable in vitro. Furthermore, overexpression of a phosphatidylinositol phosphate 5-kinase results in reduction of AVR3a levels in planta. Our results suggest that the PIP-binding ability of the AVR3a effector domain is essential for its accumulation inside host cells to suppress CMPG1-dependent immunity.</div>
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<Abstract><AbstractText>The oomycete pathogen Phytophthora infestans causes potato late blight, one of the most economically damaging plant diseases worldwide. P. infestans produces AVR3a, an essential modular virulence effector with an N-terminal RXLR domain that is required for host-cell entry. In host cells, AVR3a stabilizes and inhibits the function of the E3 ubiquitin ligase CMPG1, a key factor in host immune responses including cell death triggered by the pathogen-derived elicitor protein INF1 elicitin. To elucidate the molecular basis of AVR3a effector function, we determined the structure of Phytophthora capsici AVR3a4, a close homolog of P. infestans AVR3a. Our structural and functional analyses reveal that the effector domain of AVR3a contains a conserved, positively charged patch and that this region, rather than the RXLR domain, is required for binding to phosphatidylinositol monophosphates (PIPs) in vitro. Mutations affecting PIP binding do not abolish AVR3a recognition by the resistance protein R3a but reduce its ability to suppress INF1-triggered cell death in planta. Similarly, stabilization of CMPG1 in planta is diminished by these mutations. The steady-state levels of non-PIP-binding mutant proteins in planta are reduced greatly, although these proteins are stable in vitro. Furthermore, overexpression of a phosphatidylinositol phosphate 5-kinase results in reduction of AVR3a levels in planta. Our results suggest that the PIP-binding ability of the AVR3a effector domain is essential for its accumulation inside host cells to suppress CMPG1-dependent immunity.</AbstractText>
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<name sortKey="Kigawa, Takanori" sort="Kigawa, Takanori" uniqKey="Kigawa T" first="Takanori" last="Kigawa">Takanori Kigawa</name>
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	Serveur d'exploration sur les effecteurs du phytophthora
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Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity.

Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity.

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