New strokes to the portrait of inactivated actin

In addition to the well-known monomeric and polymeric forms of actin there is another unique thermodynamically stable state of this protein, called "inactivated actin" (I-actin). I-actin is formed at moderate concentration of a denaturant, release of Ca²⁺ ions and/or ATP, or after heating. This state is a monodisperse associate and it has the same spectral characteristics regardless of the method of preparation. The interest in I-actin arises from the discovery of similar-sized short oligomers of actin in the cell nucleus, which structurally differ from polymeric actin. In this work, we investigated the intramolecular mobility of I-actin using the time-resolved anisotropy method. Our findings indicate that its tryptophan residues participate in structural oscillations, although their correlation time is significantly longer than that of native actin. Using the dynamic light scattering, we demonstrated that I-actin obtained by heating possesses the same dimensions as I-actin in 1.8 M GdnHCl. Using the fluorescent probe ANS, it was shown that I-actin has a unique structure with hydrophobic pockets on the surface and tryptophan residues in the polar internal regions of the structure.