Open AccessProteomic identification of potential target proteins regulated by the SCF F bp1 ‐mediated proteolysis pathway in F usarium oxysporum
Author(s) -
MiguelRojas Cristina,
Hera Concepcion
Publication year - 2013
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1111/mpp.12060
Subject(s) - biology , mutant , gel electrophoresis , proteolysis , f box protein , proteasome , fusarium oxysporum , mycelium , microbiology and biotechnology , biochemistry , ubiquitin , ubiquitin ligase , botany , gene , enzyme
Summary F‐box proteins function in the recruitment of proteins for SCF ubiquitination and proteasome degradation. Here, we studied the role of F bp1, a nonessential F ‐box protein of the tomato pathogen F usarium oxysporum f. sp. lycopersici . The Δ fbp1 mutant showed a significant delay in the production of wilt symptoms on tomato plants and was impaired in invasive growth on cellophane membranes and on living plant tissue. To search for target proteins recruited by F bp1, a combination of sodium dodecylsulphate‐polyacrylamide gel electrophoresis ( SDS‐PAGE ) and matrix‐assisted laser desorption/ionization time‐of‐flight/time‐of‐flight ( MALDI‐TOF / TOF ) was used to compare proteins in mycelia of the wild‐type and Δ fbp1 mutant. The proteomic approach identified 41 proteins differing significantly in abundance between the two strains, 17 of which were more abundant in the Δ fbp1 mutant, suggesting a possible regulation by proteasome degradation. Interestingly, several of the identified proteins were related to vesicle trafficking. Microscopic analysis revealed an impairment of the Δ fbp1 strain in directional growth and in the structure of the S pitzenkörper, suggesting a role of F bp1 in hyphal orientation. Our results indicate that F bp1 regulates protein turnover and pathogenicity in F . oxysporum .