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F1000 » Evaluated Articles » Fungal virulence and development is regulated by alternative pre-mRNA 3'end processing in Magnaporthe oryzae
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Fungal virulence and development is regulated by alternative
pre-mRNA 3'end processing in Magnaporthe oryzae.
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Franceschetti M, Bueno E, Wilson RA, Tucker SL, Gómez-Mena C, Calder G, Sesma A.
PLoS Pathog. 2011 Dec; 7(12):e1002441
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Guilhem Janbon, Institut Pasteur, France. F1000 Microbiology
16 Jan 2012 | New Finding
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In this very innovative study, the authors identified an RNA-binding protein (RBP35) as a major regulator of
Magnaporthe oryzae virulence.
M. oryzae is a very important plant pathogen and is responsible for large amounts of rice and wheat culture
destruction every year that is associated with major economical losses. Although a large number of factors have
been previously shown to be implicated in this filamentous fungal virulence, this is the first time that this kind of
protein has been identified as playing a central role in this process. The results presented in this report suggest that
Rbp35 could act as a regulator of 3' end UTR length of a subset of virulence-associated genes. Importantly, the
rbp35 mutants are affected in the TOR pathway and displayed altered expression of genes coding for cell wall or
secreted proteins. This report confirms the intuitive idea that post-transcriptional regulation of gene expression can
regulate virulence, and most certainly opens new fields in the study of fungal pathogens.
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F1000 » Evaluated Articles » Fungal virulence and development is regulated by alternative pre-mRNA 3'end processing in Magnaporthe oryzae
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6
Fungal virulence and development is regulated by alternative
pre-mRNA 3'end processing in Magnaporthe oryzae.
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Franceschetti M, Bueno E, Wilson RA, Tucker SL, Gómez-Mena C, Calder G, Sesma A.
PLoS Pathog. 2011 Dec; 7(12):e1002441
Full text in journal
Available on: PubMed | Google Scholar
Evaluations 1
Comments 0
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RNA-binding proteins play a central role in post-transcriptional mechanisms that control gene expression.
Identification of novel RNA-binding proteins in fungi is essential to unravel post-transcriptional networks and cellular
processes that confer identity to the fungal kingdom. Here, we carried out the functional characterisation of the
filamentous fungus-specific RNA-binding protein RBP35 required for full virulence and development in the rice blast
fungus. RBP35 contains an N-terminal RNA recognition motif (RRM) and six Arg-Gly-Gly tripeptide repeats.
Immunoblots identified two RBP35 protein isoforms that show a steady-state nuclear localisation and bind RNA in
vitro. RBP35 coimmunoprecipitates in vivo with Cleavage Factor I (CFI) 25 kDa, a highly conserved protein involved
in polyA site recognition and cleavage of pre-mRNAs. Several targets of RBP35 have been identified using
transcriptomics including 14-3-3 pre-mRNA, an important integrator of environmental signals. In Magnaporthe
oryzae, RBP35 is not essential for viability but regulates the length of 3'UTRs of transcripts with developmental and
virulence-associated functions. The Δrbp35 mutant is affected in the TOR (target of rapamycin) signaling pathway
showing significant changes in nitrogen metabolism and protein secretion. The lack of clear RBP35 orthologues in
yeast, plants and animals indicates that RBP35 is a novel auxiliary protein of the polyadenylation machinery of
filamentous fungi. Our data demonstrate that RBP35 is the fungal equivalent of metazoan CFI 68 kDa and suggest
the existence of 3'end processing mechanisms exclusive to the fungal kingdom.
DOI: 10.1371/journal.ppat.1002441
PMID: 22194688
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