RT Journal Article
T1 Structure-activity relationship of α mating pheromone from the fungal pathogen Fusarium oxysporum
A1 Vitale, Stefania
A1 Partida Hanon, Angelica
A1 Serrano, Soraya
A1 Martínez Del Pozo, Álvaro
A1 Di Pietro, Antonio
A1 Turrà, David
A1 Bruix, Marta
AB During sexual development, ascomycete fungi produce two types of peptide pheromones termed a and α. The α 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 α pheromones from filamentous ascomycetes, which are significantly shorter and share almost no sequence similarity with the S. cerevisiae homolog. High-resolution structure of synthetic α-pheromone from the plant pathogenic ascomycete Fusarium oxysporum revealed the presence of a central β-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 α-pheromone was independent of the cognate GPCR Ste2 and of the central β-turn but instead required two conserved Trp1-Cys2 residues at the N-terminus. These results indicate that, in spite of their reduced size, fungal α-pheromones contain discrete functional regions with a defined secondary structure that regulate diverse biological processes such as polarity reorientation and cell division.
PB The American Society for Biochemistry and Molecular Biology
SN 1083-351X
YR 2017
FD 2017-01
LK https://hdl.handle.net/20.500.14352/17659
UL https://hdl.handle.net/20.500.14352/17659
LA eng
NO Unión Europea. FP7
NO Ministerio de Economía y Competitividad (MINECO)
DS Docta Complutense
RD 18 abr 2025