MelampsoraV2, Main, Merge, bibRecord, 000605

Rust fungal effectors mimic host transit peptides to translocate into chloroplasts.

Identifieur interne : 000605 ( Main/Merge ); précédent : 000604; suivant : 000606

Rust fungal effectors mimic host transit peptides to translocate into chloroplasts.

Auteurs : Benjamin Petre [Royaume-Uni, France] ; Cécile Lorrain [Royaume-Uni, France] ; Diane G O. Saunders [Royaume-Uni] ; Joe Win [Royaume-Uni] ; Jan Sklenar [Royaume-Uni] ; Sébastien Duplessis [France] ; Sophien Kamoun [Royaume-Uni]

Source :

Cellular microbiology [ 1462-5822 ] ; 2016.

RBID : pubmed:26426202

Descripteurs français

KwdFr :
- Basidiomycota (physiologie), Chloroplastes (métabolisme), Facteurs de virulence (métabolisme), Maladies des plantes (microbiologie), Mimétisme moléculaire (MeSH), Populus (microbiologie), Protéines fongiques (métabolisme), Transport des protéines (MeSH).
MESH :
- microbiologie : Maladies des plantes, Populus.
- métabolisme : Chloroplastes, Facteurs de virulence, Protéines fongiques.
- physiologie : Basidiomycota.
- Mimétisme moléculaire, Transport des protéines.

English descriptors

KwdEn :
- Basidiomycota (physiology), Chloroplasts (metabolism), Fungal Proteins (metabolism), Molecular Mimicry (MeSH), Plant Diseases (microbiology), Populus (microbiology), Protein Transport (MeSH), Virulence Factors (metabolism).
MESH :
- chemical , metabolism : Fungal Proteins, Virulence Factors.
- metabolism : Chloroplasts.
- microbiology : Plant Diseases, Populus.
- physiology : Basidiomycota.
- Molecular Mimicry, Protein Transport.

Abstract

Parasite effector proteins target various host cell compartments to alter host processes and promote infection. How effectors cross membrane-rich interfaces to reach these compartments is a major question in effector biology. Growing evidence suggests that effectors use molecular mimicry to subvert host cell machinery for protein sorting. We recently identified chloroplast-targeted protein 1 (CTP1), a candidate effector from the poplar leaf rust fungus Melampsora larici-populina that carries a predicted transit peptide and accumulates in chloroplasts and mitochondria. Here, we show that the CTP1 transit peptide is necessary and sufficient for accumulation in the stroma of chloroplasts. CTP1 is part of a Melampsora-specific family of polymorphic secreted proteins. Two members of that family, CTP2 and CTP3, also translocate in chloroplasts in an N-terminal signal-dependent manner. CTP1, CTP2 and CTP3 are cleaved when they accumulate in chloroplasts, while they remain intact when they do not translocate into chloroplasts. Our findings reveal that fungi have evolved effector proteins that mimic plant-specific sorting signals to traffic within plant cells.

Url:

https://hal.archives-ouvertes.fr/hal-02548525

DOI: 10.1111/cmi.12530
PubMed: 26426202

Links to Exploration step

pubmed:26426202

Le document en format XML

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<front><div type="abstract" xml:lang="en">Parasite effector proteins target various host cell compartments to alter host processes and promote infection. How effectors cross membrane-rich interfaces to reach these compartments is a major question in effector biology. Growing evidence suggests that effectors use molecular mimicry to subvert host cell machinery for protein sorting. We recently identified chloroplast-targeted protein 1 (CTP1), a candidate effector from the poplar leaf rust fungus Melampsora larici-populina that carries a predicted transit peptide and accumulates in chloroplasts and mitochondria. Here, we show that the CTP1 transit peptide is necessary and sufficient for accumulation in the stroma of chloroplasts. CTP1 is part of a Melampsora-specific family of polymorphic secreted proteins. Two members of that family, CTP2 and CTP3, also translocate in chloroplasts in an N-terminal signal-dependent manner. CTP1, CTP2 and CTP3 are cleaved when they accumulate in chloroplasts, while they remain intact when they do not translocate into chloroplasts. Our findings reveal that fungi have evolved effector proteins that mimic plant-specific sorting signals to traffic within plant cells. </div>
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<author><name sortKey="Win, Joe" sort="Win, Joe" uniqKey="Win J" first="Joe" last="Win">Joe Win</name>
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<author><name sortKey="Sklenar, Jan" sort="Sklenar, Jan" uniqKey="Sklenar J" first="Jan" last="Sklenar">Jan Sklenar</name>
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<series><title level="j">Cellular microbiology</title>
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<term>Chloroplasts (metabolism)</term>
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<term>Molecular Mimicry (MeSH)</term>
<term>Plant Diseases (microbiology)</term>
<term>Populus (microbiology)</term>
<term>Protein Transport (MeSH)</term>
<term>Virulence Factors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (physiologie)</term>
<term>Chloroplastes (métabolisme)</term>
<term>Facteurs de virulence (métabolisme)</term>
<term>Maladies des plantes (microbiologie)</term>
<term>Mimétisme moléculaire (MeSH)</term>
<term>Populus (microbiologie)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Transport des protéines (MeSH)</term>
</keywords>
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</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Maladies des plantes</term>
<term>Populus</term>
</keywords>
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<term>Populus</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Parasite effector proteins target various host cell compartments to alter host processes and promote infection. How effectors cross membrane-rich interfaces to reach these compartments is a major question in effector biology. Growing evidence suggests that effectors use molecular mimicry to subvert host cell machinery for protein sorting. We recently identified chloroplast-targeted protein 1 (CTP1), a candidate effector from the poplar leaf rust fungus Melampsora larici-populina that carries a predicted transit peptide and accumulates in chloroplasts and mitochondria. Here, we show that the CTP1 transit peptide is necessary and sufficient for accumulation in the stroma of chloroplasts. CTP1 is part of a Melampsora-specific family of polymorphic secreted proteins. Two members of that family, CTP2 and CTP3, also translocate in chloroplasts in an N-terminal signal-dependent manner. CTP1, CTP2 and CTP3 are cleaved when they accumulate in chloroplasts, while they remain intact when they do not translocate into chloroplasts. Our findings reveal that fungi have evolved effector proteins that mimic plant-specific sorting signals to traffic within plant cells. </div>
</front>
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Serveur d'exploration Melampsora (ISTEX)

Rust fungal effectors mimic host transit peptides to translocate into chloroplasts.

Rust fungal effectors mimic host transit peptides to translocate into chloroplasts.

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