* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Download F1000 - CBGP
Survey
Document related concepts
Protein design wikipedia , lookup
Homology modeling wikipedia , lookup
Protein domain wikipedia , lookup
List of types of proteins wikipedia , lookup
Intrinsically disordered proteins wikipedia , lookup
Protein folding wikipedia , lookup
Protein structure prediction wikipedia , lookup
Bimolecular fluorescence complementation wikipedia , lookup
Protein mass spectrometry wikipedia , lookup
Western blot wikipedia , lookup
Nuclear magnetic resonance spectroscopy of proteins wikipedia , lookup
Protein purification wikipedia , lookup
Transcript
F1000 » Evaluated Articles » Fungal virulence and development is regulated by alternative pre-mRNA 3'end processing in Magnaporthe oryzae F1000 F1000 Posters Welcome Ane S Galarraga F1000 Research Sign out Evaluated Articles Evaluated Articles Advanced Search Evaluated Articles Rankings Reports Faculty Naturally Selected MyF1000 About Subscribe F1000 » Evaluated Articles » 6 Fungal virulence and development is regulated by alternative pre-mRNA 3'end processing in Magnaporthe oryzae. Bookmark to MyF1000 Export Article Links and Sharing 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 Related Evaluated Articles Abstract Retrieve article from: More Options Guilhem Janbon, Institut Pasteur, France. F1000 Microbiology 16 Jan 2012 | New Finding 6 RECOMMENDED 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. Competing interests None declared Cite this evaluation Cite this page Relevant Sections F1000 » Evaluated Articles » Fungal virulence and development is regulated by alternative pre-mRNA 3'end processing in Magnaporthe oryzae F1000 F1000 Posters Welcome Ane S Galarraga F1000 Research Sign out Evaluated Articles Evaluated Articles Advanced Search Evaluated Articles Rankings Reports Faculty Naturally Selected MyF1000 About Subscribe F1000 » Evaluated Articles » 6 Fungal virulence and development is regulated by alternative pre-mRNA 3'end processing in Magnaporthe oryzae. Bookmark to MyF1000 Export Article Links and Sharing 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 Related Evaluated Articles Abstract Retrieve article from: More Options 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 Relevant Sections