Fig. 3: Interdomain persistent length modulates DIAPH1 activity.
From: Negative cooperativity regulates ligand activation of DIAPH1 and other diaphanous related formins
A Plot of the radius of gyration, RG, versus the number of amino acids in a theoretical polypeptide. The parameter ν characterizes the dimensions of the amino acid chain where 0.60, red, represents an expanded coil and 0.30, maroon, represents the most compact globule state. B Monte-Carlo simulation using ν = 0.60 showing the theoretical persistence length between DID and DAD domains as a function of the number of amino acids: ~109 Å for the 285 amino acid DIAPH1 and ~90 Å for the 140 amino acids of DIAPH1/2. C Rates of actin polymerization for Diaphanous constructs DIAPH1, D1, DIAPH1/2, D1/2 and DIAPH1ΔDAD, D1ΔD, in the presence of RhoA, +R, compared to actin alone, A. Initial rates of polymerization, dF/dt, were determined by fitting the first 11 data points to a linear equation yielding slopes of 62 ± 6 AFU*s−1 for A (red), 66 ± 6 AFU*s−1 for D1 (green), 62 ± 7 AFU*s−1 for D1/2 (purple), 85 ± 5 AFU*s−1 for D1 + R (white), 75 ± 4 AFU*s-1 for D1/2 + R (gray) and 104 ± 7 AFU*s−1 for D1 ΔD (orange). D1ΔD represents 100% activation and D1 or D1/2 represent 0% activation, respectively. Statistical p-values at 95% confidence are shown on the graph and all values are represented as mean ± SD derived from N = 3 independent experiments.
