The gated gait of the processive molecular motor, myosin V View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-01

AUTHORS

Claudia Veigel, Fei Wang, Marc L Bartoo, James R Sellers, Justin E Molloy

ABSTRACT

Class V myosins are actin-based molecular motors involved in vesicular and organellar transport. Single myosin V molecules move processively along F-actin, taking several 36-nm steps for each diffusional encounter. Here we have measured the mechanical interactions between mouse brain myosin V and rabbit skeletal F-actin. The working stroke produced by a myosin V head is approximately 25 nm, consisting of two separate mechanical phases (20 + 5 nm). We show that there are preferred myosin binding positions (target zones) every 36 nm along the actin filament, and propose that the 36-nm steps of the double-headed motor are a combination of the working stroke (25 nm) of the bound head and a biased, thermally driven diffusive movement (11 nm) of the free head onto the next target zone. The second phase of the working stroke (5 nm) acts as a gate - like an escapement in a clock, coordinating the ATPase cycles of the two myosin V heads. This mechanism increases processivity and enables a single myosin V molecule to travel distances of several hundred nanometres along the actin filament. More... »

PAGES

59-65

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncb732

DOI

http://dx.doi.org/10.1038/ncb732

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050964253

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11740494


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