Switch between large hand-over-hand and small inchworm-like steps in myosin VI.
Many biological motor molecules move within cells using stepsizes predictable from their structures. Myosin VI, however, has much larger and more broadly distributed stepsizes than those predicted from its short lever arms. We explain the discrepancy by monitoring Qdots and gold nanoparticles attached to the myosin-VI motor domains using high-sensitivity nanoimaging. The large stepsizes were attributed to an extended and relatively rigid lever arm; their variability to two stepsizes, one large (72 nm) and one small (44 nm). These results suggest that there exist two tilt angles during myosin-VI stepping, which correspond to the pre- and postpowerstroke states and regulate the leading head. The large steps are consistent with the previously reported hand-over-hand mechanism, while the small steps follow an inchworm-like mechanism and increase in frequency with ADP. Switching between these two mechanisms in a strain-sensitive, ADP-dependent manner allows myosin VI to fulfill its multiple cellular tasks including vesicle transport and membrane anchoring.
Nishikawa
So
S
Graduate School of Frontier Biosciences, Osaka University, Yamadaoka, Suita, Osaka 565-0871, Japan.
Arimoto
Ikuo
I
Ikezaki
Keigo
K
Sugawa
Mitsuhiro
M
Ueno
Hiroshi
H
Komori
Tomotaka
T
Iwane
Atsuko H
AH
Yanagida
Toshio
T
D000199:Actins / Q000378:metabolism; D000818:Animals; D002645:Chickens; D019281:Dimerization; D006046:Gold; D006801:Humans; D053768:Metal Nanoparticles; D008853:Microscopy; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D008958:Models, Molecular; D018995:Myosin Heavy Chains / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D045663:Quantum Dots
D000199:Actins; C089785:myosin VI; D006046:Gold; D018995:Myosin Heavy Chains