Journal: Scientific Reports

Article Title: Conservation of Cdc14 phosphatase specificity in plant fungal pathogens: implications for antifungal development

doi: 10.1038/s41598-020-68921-3

Figure Lengend Snippet: Fungal Cdc14 homologs can be specifically inhibited by a substrate mimetic. ( a ) Structure of the synthetic peptide used for inhibition assays (sequence Glu-Val-pCF 2 Ser-Pro-Thr-Lys-Arg-amide). ( b ) Dose response with the pCF 2 Ser peptide from A and the indicated fungal Cdc14 enzymes using DiFMUP as substrate. Data represent the average of 5 or 6 independent trials. It was not practical to show error bars on the graph, however error values for replicate K i measurements are provided in ( c ). Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism. We did not have enough pCF 2 Ser peptide to perform the full analysis on all 8 plant fungal pathogen homologs. ( c ) Each individual trial from the experiment in ( b ) was fit as described in b to generate IC 50 , from which K i was calculated (see “ ”). Values represent the mean ± standard deviation. ( d ) Comparison of pCF 2 Ser peptide inhibition of human tyrosine phosphatase PTP1B and dual specificity phosphatase VHR to ScCdc14 and human Cdc14A using DiFMUP at the measured K M for each enzyme. Percent activity relative to a no inhibitor control was calculated and plotted. Data are means of 3 independent experiments and error bars are standard deviations. Numbers over the bars are p values from a t- test (unpaired, one-tail) comparing 0 and 200 µM inhibitor data.

Article Snippet: Best fit lines were generated with a standard slope dose response function with plateaus set at 100% and 0% in Graphpad Prism.

Techniques: Inhibition, Sequencing, Generated, Standard Deviation, Comparison, Activity Assay, Control