BD SIMULATIONS OF THE IONIC STRENGTH DEPENDENCE OF THE INTERACTIONS BETWEEN TRIOSE PHOSPHATE ISOMERASE AND F-ACTIN

Functional protein-protein interactions are essential for many physiological processes. For example, the association of glycolytic enzymes to F-actin is proposed to be one mechanism through which glycolytic enzymes are compartmentalized, and as a result, play essential roles such as regulation of the glycolytic pathway and increasing glycolytic flux. Many glycolytic enzymes including fructose-1,6-bisphophate aldolase, glyceraldedhye-3-phosphate dehydrogenase, and lactate dehydrogenase bind F-actin strongly. Other glycolytic enzymes including triose phosphate isomerase (TPI) do not interact with F-actin significantly. Herein, Brownian dynamics (BD) simulations determine the energetics of the association of F-actin with the glycolytic enzyme triose phosphate isomerase as a function of ionic strength. This is the first thorough control study examining how well BD reproduces the experimental observations that the binding of TPI to F-actin is very weak and falls off rapidly as ionic strength increases. The BD results confirm experimental observations that the degree of association diminishes as ionic strength increases and that the interaction of TPI with F-actin is weakly nonspecific to nonexistent.