Abstract
One of the most abundant proteins in eukaryotes is actin, a ubiquitous protein that plays a role in cell dynamics like cell migration. The dynamics of actin filament treadmilling is regulated by two actin structural states: globular actin (G-actin) and filamentous actin (F-actin). Although recently it was reported that the structure of the two actins differ (Oda., et al, Fujii., et al), there is still much to resolve on the matter of their dynamic structures.Here we observed the dynamics of the actin structural states under various conditions by using single-molecule FRET in combination with TIRF microscopy. We found that bothF-actin and G-actin have at least two distinct states, and that the population distribution of these states depends on the ionic conditions.Furthermore, these states were sensitive to actin binding proteins like myosin and actinin. We are currently investigating actin structural states by performing FRET measurements to observe various positions of actin in the presence of the actin binding proteins myosins.
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