A single molecule of F1-ATPase has been shown to be the smallest rotary motor ever found, with a central rotor of radius ~1 nm turning in a stator barrel of radius ~5 nm. Continuous rotation of the central γ subunit was revealed under an optical microscope by attaching to γ a huge marker, an actin filament. In a separate study, rotation of a sliding actin filament around its axis has been revealed by attaching a small probe, a single fluorescent dye molecule, to the actin filament and detecting the orientation of the fluorophore, and thus of the actin filament, through polarization imaging. The axial rotation was slow compared to the linear sliding, indicating that myosin does not 'walk' along the helical array of actin protomers but 'runs,' skipping many protomers. The two motors above, one rotary and the other linear, represent two extreme cases of the mode of motor operation: in the F1-ATPase the two partners, the rotor and stator, never detach from each other whereas myosin touches actin only occasionally. In considering the mechanisms of these and other molecular motors, distinction between bending and binding is important. The use of huge and small probes as described above should be useful in studies of protein machines in general, as a means of detecting conformational changes in a single protein molecule during function.
|Number of pages||10|
|Journal||Advances in Experimental Medicine and Biology|
|Publication status||Published - 1998|
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)