The motor domain determines the large step of myosin-V View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-01

AUTHORS

Hiroto Tanaka, Kazuaki Homma, Atsuko Hikikoshi Iwane, Eisaku Katayama, Reiko Ikebe, Junya Saito, Toshio Yanagida, Mitsuo Ikebe

ABSTRACT

Class-V myosin proceeds along actin filaments with large (∼36 nm) steps1,2,3. Myosin-V has two heads, each of which consists of a motor domain and a long (23 nm) neck domain. In accordance with the widely accepted lever-arm model4, it was suggested that myosin-V steps to successive (36 nm) target zones along the actin helical repeat by tilting its long neck (lever-arm)5. To test this hypothesis, we measured the mechanical properties of single molecules of myosin-V truncation mutants with neck domains only one-sixth of the native length. Our results show that the processivity and step distance along actin are both similar to those of full-length myosin-V. Thus, the long neck domain is not essential for either the large steps or processivity of myosin-V. These results challenge the lever-arm model. We propose that the motor domain and/or the actomyosin interface enable myosin-V to produce large processive steps during translocation along actin. More... »

PAGES

192-195

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/415192a

DOI

http://dx.doi.org/10.1038/415192a

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1015782024

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11805840


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