| Title: | Structure-Activity Relationship of alpha Mating Pheromone from the Fungal Pathogen Fusarium oxysporum |
| Author(s): | Vitale S; Partida-Hanon A; Serrano S; Martinez-Del-Pozo A; Di Pietro A; Turra D; Bruix M; |
| Address: | "From the Department of Genetics, Campus de Excelencia Internacional Agroalimentario ceiA3, Universidad de Cordoba, 14071 Cordoba, Spain. the Department of Biological Physical Chemistry, Institute of Physical Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain, and. the Department of Biochemistry and Molecular Biology I, Faculty of Chemistry, Complutense University, 28040 Madrid, Spain. From the Department of Genetics, Campus de Excelencia Internacional Agroalimentario ceiA3, Universidad de Cordoba, 14071 Cordoba, Spain, ge3tutud@uco.es. the Department of Biological Physical Chemistry, Institute of Physical Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain, and mbruix@iqfr.csic.es" |
| ISSN/ISBN: | 1083-351X (Electronic) 0021-9258 (Print) 0021-9258 (Linking) |
| Abstract: | "During sexual development ascomycete fungi produce two types of peptide pheromones termed a and alpha. The alpha pheromone from the budding yeast Saccharomyces cerevisiae, a 13-residue peptide that elicits cell cycle arrest and chemotropic growth, has served as paradigm for the interaction of small peptides with their cognate G protein-coupled receptors. However, no structural information is currently available for alpha pheromones from filamentous ascomycetes, which are significantly shorter and share almost no sequence similarity with the S. cerevisiae homolog. High resolution structure of synthetic alpha-pheromone from the plant pathogenic ascomycete Fusarium oxysporum revealed the presence of a central beta-turn resembling that of its yeast counterpart. Disruption of the-fold by d-alanine substitution of the conserved central Gly(6)-Gln(7) 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 alpha-pheromone was independent of the cognate G protein-coupled receptors Ste2 and of the central beta-turn but instead required two conserved Trp(1)-Cys(2) residues at the N terminus. These results indicate that, despite their reduced size, fungal alpha-pheromones contain discrete functional regions with a defined secondary structure that regulate diverse biological processes such as polarity reorientation and cell division" |
| Keywords: | "Cell Cycle Cell Nucleus/metabolism Chemotactic Factors/*chemistry Cysteine/chemistry Fungal Proteins/*chemistry Fusarium/*chemistry Genes, Mating Type, Fungal Peptides/chemistry Pheromones/*chemistry Protein Domains Protein Structure, Secondary Receptors, ;" |
| Notes: | "MedlineVitale, Stefania Partida-Hanon, Angelica Serrano, Soraya Martinez-Del-Pozo, Alvaro Di Pietro, Antonio Turra, David Bruix, Marta eng 2017/01/20 J Biol Chem. 2017 Mar 3; 292(9):3591-3602. doi: 10.1074/jbc.M116.766311. Epub 2017 Jan 18" |
