β-Thymosins sequester G-actin and preserve a pool of monomers of actin which constitute an important prerequisite for cellular function of the microfilament system. To study the influence of paraquat binding to G-actin on the interaction of G-actin with thymosin β4 we determined the apparent dissociation constant of the G-actin-thymosin β4 complex in the absence or presence of paraquat using an ultrafiltration assay. Paraquat (1,1'-dimethyl-4,4'-dipyridylium dichloride) attenuates this interaction in a concentration- and time-dependent manner. When exposed to 10 mM paraquat, the apparent dissociation constant increased 10-85-fold within 15 min to 24 h. After incubation for 24 h even a paraquat concentration as low as 100 μM increased the dissociation constant of the G-actin-thymosin β4 complex from 0.66 μM to 0.82 μM (P < 0.05). Diquat (1,1'-ethylene-2,2'-dipyridylium dibromide) similarly weakens the interaction of G-actin and β-thymosins. In none of the experiments was oxidation of the methionine residue or any other modification of thymosin β4 detected. Therefore we conclude that the dipyridyls paraquat and diquat directly interact with G-actin and thereby impede the interaction between G-actin and thymosin β4.
Huff, T., Cappelletti, G., & Hannappel, E. (1998). The dipyridyls paraquat and diquat attenuate the interaction of G-actin with thymosin β4. FEBS Letters, 425(3), 495–498. https://doi.org/10.1016/S0014-5793(98)00295-6