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Título:
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Structure-activity relationship of ? mating pheromone from the fungal pathogen Fusarium oxysporum
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Autores:
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Vitale, Stefania ;
Partida Hanon, Angélica ;
Serrano, Soraya ;
Martínez del Pozo, Álvaro ;
Di Pietro, Antonio ;
Turrà, David ;
Bruix, Marta
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Tipo de documento:
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texto impreso
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Editorial:
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The American Society for Biochemistry and Molecular Biology, 2017-01
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias: Química: Biología molecular
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Materia = Ciencias: Química: Bioquímica
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Tipo = Artículo
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Resumen:
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During sexual development, ascomycete fungi produce two types of peptide pheromones termed a and ?. The ? pheromone from the budding yeast Saccharomyces cerevisiae, a thirteen residue peptide which elicits cell cycle arrest and chemotropic growth, has served as paradigm for the interaction of small peptides with their cognate G protein-coupled receptors (GPCRs). However, no structural information is currently available for ? pheromones from filamentous ascomycetes, which are significantly shorter and share almost no sequence similarity with the S. cerevisiae homolog. High-resolution structure of synthetic ?-pheromone from the plant pathogenic ascomycete Fusarium oxysporum revealed the presence of a central ?-turn resembling that of its yeast counterpart. Disruption of the fold by Dalanine substitution of the conserved central Gly6-Gln7 residues or by random sequence scrambling demonstrated a crucial role for this structural determinant in chemoattractant activity. Unexpectedly, the growth inhibitory effect of F. oxysporum ?-pheromone was independent of the cognate GPCR Ste2 and of the central ?-turn but instead required two conserved Trp1-Cys2 residues at the N-terminus. These results indicate that, in spite of their reduced size, fungal ?-pheromones contain discrete functional regions with a defined secondary structure that regulate diverse biological processes such as polarity reorientation and cell division.
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En línea:
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https://eprints.ucm.es/id/eprint/41589/1/J.%20Biol.%20Chem.-2017-Vitale-jbc.M116.766311%28Alvaro%29.pdf
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