RustEffectorV1, Main, Exploration, bibRecord, 000111

The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.

Identifieur interne : 000111 ( Main/Exploration ); précédent : 000110; suivant : 000112

The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.

Auteurs : Klara Pretsch [Allemagne] ; Ariane Kemen ; Eric Kemen ; Matthias Geiger ; Kurt Mendgen ; Ralf Voegele

Source :

Molecular plant pathology [ 1364-3703 ] ; 2013.

RBID : pubmed:22998218

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (drug effects), Basidiomycota (metabolism), Cysteine Proteinase Inhibitors (chemistry), Cysteine Proteinase Inhibitors (pharmacology), Disulfides (metabolism), Exons (genetics), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Fungal Proteins (pharmacology), Introns (genetics), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Pichia (drug effects), Pichia (metabolism), Protease Inhibitors (chemistry), Protease Inhibitors (metabolism), Protease Inhibitors (pharmacology), Protein Stability (drug effects), Protein Structure, Tertiary (MeSH), Proteolysis (drug effects), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , chemistry : Cysteine Proteinase Inhibitors, Fungal Proteins, Protease Inhibitors.
- drug effects : Basidiomycota, Pichia, Protein Stability, Proteolysis.
- genetics : Exons, Introns.
- metabolism : Basidiomycota, Disulfides, Fungal Proteins, Pichia, Protease Inhibitors.
- chemical , pharmacology : Cysteine Proteinase Inhibitors, Fungal Proteins, Protease Inhibitors.
- Amino Acid Sequence, Molecular Sequence Data, Phylogeny, Protein Structure, Tertiary, Sequence Alignment, Sequence Homology, Amino Acid.

Abstract

Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N-terminus and a conserved and structured C-terminus. The characterization of Uf-RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C-terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf-RTP1p and Us-RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi-specific family of modular effector proteins comprising an unstructured N-terminal domain and a structured C-terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.

DOI: 10.1111/j.1364-3703.2012.00832.x
PubMed: 22998218
PubMed Central: PMC6638633

Affiliations:

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

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Le document en format XML

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<term>Basidiomycota (metabolism)</term>
<term>Cysteine Proteinase Inhibitors (chemistry)</term>
<term>Cysteine Proteinase Inhibitors (pharmacology)</term>
<term>Disulfides (metabolism)</term>
<term>Exons (genetics)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Fungal Proteins (pharmacology)</term>
<term>Introns (genetics)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Pichia (drug effects)</term>
<term>Pichia (metabolism)</term>
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<term>Protease Inhibitors (metabolism)</term>
<term>Protease Inhibitors (pharmacology)</term>
<term>Protein Stability (drug effects)</term>
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<term>Proteolysis (drug effects)</term>
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<term>Disulfures (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Exons (génétique)</term>
<term>Inhibiteurs de la cystéine protéinase (composition chimique)</term>
<term>Inhibiteurs de la cystéine protéinase (pharmacologie)</term>
<term>Inhibiteurs de protéases (composition chimique)</term>
<term>Inhibiteurs de protéases (métabolisme)</term>
<term>Inhibiteurs de protéases (pharmacologie)</term>
<term>Introns (génétique)</term>
<term>Phylogenèse (MeSH)</term>
<term>Pichia (effets des médicaments et des substances chimiques)</term>
<term>Pichia (métabolisme)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines fongiques (pharmacologie)</term>
<term>Protéolyse (effets des médicaments et des substances chimiques)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Stabilité protéique (effets des médicaments et des substances chimiques)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Basidiomycota</term>
<term>Pichia</term>
<term>Protein Stability</term>
<term>Proteolysis</term>
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<term>Introns</term>
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<term>Disulfides</term>
<term>Fungal Proteins</term>
<term>Pichia</term>
<term>Protease Inhibitors</term>
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<term>Protéines fongiques</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de la cystéine protéinase</term>
<term>Inhibiteurs de protéases</term>
<term>Protéines fongiques</term>
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<term>Protease Inhibitors</term>
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<term>Molecular Sequence Data</term>
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<term>Données de séquences moléculaires</term>
<term>Phylogenèse</term>
<term>Similitude de séquences d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N-terminus and a conserved and structured C-terminus. The characterization of Uf-RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C-terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf-RTP1p and Us-RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi-specific family of modular effector proteins comprising an unstructured N-terminal domain and a structured C-terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.</div>
</front>
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<Abstract><AbstractText>Only few fungal effectors have been described to be delivered into the host cell during obligate biotrophic interactions. RTP1p, from the rust fungi Uromyces fabae and U. striatus, was the first fungal protein for which localization within the host cytoplasm could be demonstrated directly. We investigated the occurrence of RTP1 homologues in rust fungi and examined the structural and biochemical characteristics of the corresponding gene products. The analysis of 28 homologues showed that members of the RTP family are most likely to occur ubiquitously in rust fungi and to be specific to the order Pucciniales. Sequence analyses indicated that the structure of the RTPp effectors is bipartite, consisting of a variable N-terminus and a conserved and structured C-terminus. The characterization of Uf-RTP1p mutants showed that four conserved cysteine residues sustain structural stability. Furthermore, the C-terminal domain exhibits similarities to that of cysteine protease inhibitors, and it was shown that Uf-RTP1p and Us-RTP1p are able to inhibit proteolytic activity in Pichia pastoris culture supernatants. We conclude that the RTP1p homologues constitute a rust fungi-specific family of modular effector proteins comprising an unstructured N-terminal domain and a structured C-terminal domain, which exhibit protease inhibitory activity possibly associated with effector function during biotrophic interactions.</AbstractText>
<CopyrightInformation>© 2012 THE AUTHORS. MOLECULAR PLANT PATHOLOGY © 2012 BSPP AND BLACKWELL PUBLISHING LTD.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pretsch</LastName>
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<Author ValidYN="Y"><LastName>Kemen</LastName>
<ForeName>Ariane</ForeName>
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<Author ValidYN="Y"><LastName>Kemen</LastName>
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<Author ValidYN="Y"><LastName>Mendgen</LastName>
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<MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName>
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The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.

The rust transferred proteins-a new family of effector proteins exhibiting protease inhibitor function.

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