Fig. 1: SUMO2 isoform preference of SENP5CD catalytic domain.
From: Structural basis for the human SENP5’s SUMO isoform discrimination
a SDS-PAGE of the endpoint assays of SENP5 using RanGAP1-SUMO1 and RanGAP1-SUMO2 substrates. (Right) Plot of the fraction of the RanGAP1-SUMO2 substrate after 30 min reaction. Data values represent the mean ± SEM, n = 3 technical replicates. Significance was measured by a two-tailed unpaired t test relative to wild-type. All data were analyzed with a 95% confidence interval. *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001. Exact P value: 0.0003. b Plot of the proteolytic cleavage of SUMO1-AMC and SUMO2-AMC to test the activity of SENP5. SUMO2-AMC was incubated with SENP5, and released AMC was identified by fluorescence. c Plot of a competition assay by measuring the interference of the SENP5 activity for SUMO2-Rhodamine substrate by competition with either RanGAP1-SUMO1 and RanGAP1-SUMO2 at different concentrations. (Right) Inhibitory constant values for RanGAP1-SUMO1 and RanGAP-SUMO2 substrates on the SENP5 activity on SUMO2-Rho. Data values represent the mean ± SEM, n = 3 technical replicates. Source data are provided as a Source Data file.
