PoplarV1, Main, Exploration, bibRecord, 002283

Discovery of a novel small secreted protein family with conserved N-terminal IGY motif in Dikarya fungi.

Identifieur interne : 002283 ( Main/Exploration ); précédent : 002282; suivant : 002284

Discovery of a novel small secreted protein family with conserved N-terminal IGY motif in Dikarya fungi.

Auteurs : Qiang Cheng [République populaire de Chine] ; Haoran Wang ; Bin Xu ; Sheng Zhu ; Lanxi Hu ; Minren Huang

Source :

BMC genomics [ 1471-2164 ] ; 2014.

RBID : pubmed:25526808

Descripteurs français

KwdFr :
- Ascomycota (cytologie), Ascomycota (génétique), Ascomycota (métabolisme), Ascomycota (physiologie), Données de séquences moléculaires (MeSH), Génome fongique (génétique), Génomique (MeSH), Motifs d'acides aminés (MeSH), Phylogenèse (MeSH), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Similitude de séquences d'acides aminés (MeSH), Spécificité d'espèce (MeSH), Symbiose (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- composition chimique : Protéines fongiques.
- cytologie : Ascomycota.
- génétique : Ascomycota, Génome fongique, Protéines fongiques.
- métabolisme : Ascomycota, Protéines fongiques.
- physiologie : Ascomycota.
- Données de séquences moléculaires, Génomique, Motifs d'acides aminés, Phylogenèse, Régulation de l'expression des gènes fongiques, Similitude de séquences d'acides aminés, Spécificité d'espèce, Symbiose, Séquence conservée, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Ascomycota (cytology), Ascomycota (genetics), Ascomycota (metabolism), Ascomycota (physiology), Conserved Sequence (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Genome, Fungal (genetics), Genomics (MeSH), Molecular Sequence Data (MeSH), Phylogeny (MeSH), Sequence Homology, Amino Acid (MeSH), Species Specificity (MeSH), Symbiosis (MeSH).
MESH :
- chemical , chemistry : Fungal Proteins.
- cytology : Ascomycota.
- genetics : Ascomycota, Fungal Proteins, Genome, Fungal.
- metabolism : Ascomycota, Fungal Proteins.
- physiology : Ascomycota.
- Amino Acid Motifs, Amino Acid Sequence, Conserved Sequence, Gene Expression Regulation, Fungal, Genomics, Molecular Sequence Data, Phylogeny, Sequence Homology, Amino Acid, Species Specificity, Symbiosis.

Abstract

BACKGROUND

Small secreted proteins (SSPs) are employed by plant pathogenic fungi as essential strategic tools for their successful colonization. SSPs are often species-specific and so far only a few widely phylogenetically distributed SSPs have been identified.

RESULTS

A novel fungal SSP family consisting of 107 members was identified in the poplar tree fungal pathogen Marssonina brunnea, which accounts for over 17% of its secretome. We named these proteins IGY proteins (IGYPs) based on the conserved three amino acids at the N-terminus. In spite of overall low sequence similarity among IGYPs; they showed conserved N- and C-terminal motifs and a unified gene structure. By RT-PCR-seq, we analyzed the IGYP gene models and validated their expressions as active genes during infection. IGYP homologues were also found in 25 other Dikarya fungal species, all of which shared conserved motifs and the same gene structure. Furthermore, 18 IGYPs from 11 fungi also shared similar genomic contexts. Real-time RT-PCR showed that 8 MbIGYPs were highly expressed in the biotrophic stage. Interestingly, transient assay of 12 MbIGYPs showed that the MbIGYP13 protein induced cell death in resistant poplar clones.

CONCLUSIONS

In total, 154 IGYPs in 26 fungi of the Dikarya subkingdom were discovered. Gene structure and genomic context analyses indicated that IGYPs originated from a common ancestor. In M. brunnea, the expansion of highly divergent MbIGYPs possibly is associated with plant-pathogen arms race.

DOI: 10.1186/1471-2164-15-1151
PubMed: 25526808
PubMed Central: PMC4367982

Affiliations:

République populaire de Chine

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

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Le document en format XML

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<term>Similitude de séquences d'acides aminés (MeSH)</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>Small secreted proteins (SSPs) are employed by plant pathogenic fungi as essential strategic tools for their successful colonization. SSPs are often species-specific and so far only a few widely phylogenetically distributed SSPs have been identified.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>A novel fungal SSP family consisting of 107 members was identified in the poplar tree fungal pathogen Marssonina brunnea, which accounts for over 17% of its secretome. We named these proteins IGY proteins (IGYPs) based on the conserved three amino acids at the N-terminus. In spite of overall low sequence similarity among IGYPs; they showed conserved N- and C-terminal motifs and a unified gene structure. By RT-PCR-seq, we analyzed the IGYP gene models and validated their expressions as active genes during infection. IGYP homologues were also found in 25 other Dikarya fungal species, all of which shared conserved motifs and the same gene structure. Furthermore, 18 IGYPs from 11 fungi also shared similar genomic contexts. Real-time RT-PCR showed that 8 MbIGYPs were highly expressed in the biotrophic stage. Interestingly, transient assay of 12 MbIGYPs showed that the MbIGYP13 protein induced cell death in resistant poplar clones.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b>
</p>
<p>In total, 154 IGYPs in 26 fungi of the Dikarya subkingdom were discovered. Gene structure and genomic context analyses indicated that IGYPs originated from a common ancestor. In M. brunnea, the expansion of highly divergent MbIGYPs possibly is associated with plant-pathogen arms race.</p>
</div>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Small secreted proteins (SSPs) are employed by plant pathogenic fungi as essential strategic tools for their successful colonization. SSPs are often species-specific and so far only a few widely phylogenetically distributed SSPs have been identified.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">A novel fungal SSP family consisting of 107 members was identified in the poplar tree fungal pathogen Marssonina brunnea, which accounts for over 17% of its secretome. We named these proteins IGY proteins (IGYPs) based on the conserved three amino acids at the N-terminus. In spite of overall low sequence similarity among IGYPs; they showed conserved N- and C-terminal motifs and a unified gene structure. By RT-PCR-seq, we analyzed the IGYP gene models and validated their expressions as active genes during infection. IGYP homologues were also found in 25 other Dikarya fungal species, all of which shared conserved motifs and the same gene structure. Furthermore, 18 IGYPs from 11 fungi also shared similar genomic contexts. Real-time RT-PCR showed that 8 MbIGYPs were highly expressed in the biotrophic stage. Interestingly, transient assay of 12 MbIGYPs showed that the MbIGYP13 protein induced cell death in resistant poplar clones.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">In total, 154 IGYPs in 26 fungi of the Dikarya subkingdom were discovered. Gene structure and genomic context analyses indicated that IGYPs originated from a common ancestor. In M. brunnea, the expansion of highly divergent MbIGYPs possibly is associated with plant-pathogen arms race.</AbstractText>
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Discovery of a novel small secreted protein family with conserved N-terminal IGY motif in Dikarya fungi.

Discovery of a novel small secreted protein family with conserved N-terminal IGY motif in Dikarya fungi.

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