Descripción
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Rbp35 is an RNA-binding protein required for Magnaporthe oryzae?s full virulence. This protein is a novel protein component of the 3? end processing machinery present exclusively in filamentous fungi [1]. Rbp35 has six tripeptides Arg-gly-Gly (RGG) within a region that regulates nucleocytoplasmic transport and protein degradation. It has a C-terminal autoregulatory domain too. Interestingly, an additional post-transcriptional mechanism is present in Rbp35 5? leader region. Two sense and polyadenylated upstream open reading frames (uORF1 and uORF2) are found within a 233 bp intron located in the 5?UTR of the RBP35 gene. uORF1 can modulate the TOR signaling pathway in the presence of Rbp35 in trans, a surprising feature for an uORF. Furthermore, uORF1 is possibly regulating Rbp35 translation [2]. The aim of my investigation is to study Rbp35 regulation, specifically how 5?UTR uORFs can regulate Rbp35 protein levels in the fungal cell. To achieve this several approaches have been undertaken. First, uORF1 function is being analyzed by site-directed mutagenesis of its start codon and changing conserved sequences within the 5? UTR intron (donor site, acceptor site and branch point) where the uORF1 is located. Second, uORF1 is being tagged with HA to see if it can encode a functional peptide. Third, usually uORFs regulate in cis the main downstream coding sequence by non-sense mediated decay machinery. Expression of several constructs of RBP35 in the ?upf1 mutant background is being analysed to see if the presence or absence of the uORF1 and uORF1 can regulate its mRNA levels. | |
Internacional
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Si |
Nombre congreso
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Workshop New Frontiers in Plant Biology |
Tipo de participación
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970 |
Lugar del congreso
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Centro de Biotecnología y Genómica de Plantas |
Revisores
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Si |
ISBN o ISSN
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0000-0000 |
DOI
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Fecha inicio congreso
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15/06/2016 |
Fecha fin congreso
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17/06/2016 |
Desde la página
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27 |
Hasta la página
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27 |
Título de las actas
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Multilevel regulation of a protein component of the polyadenylation machinery in Magnaporthe oryzae |