Sliding movement of single actin filaments on one-headed myosin filaments View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-04-01

AUTHORS

Yoshie Harada, Akira Noguchi, Akiyoshi Kishino, Toshio Yanagida

ABSTRACT

The myosin molecule consists of two heads, each of which contains an enzymatic active site and an actin-binding site. The fundamental problem of whether the two heads function independently or cooperatively during muscle contraction has been studied by methods using an actomyosin thread1, superprecipitation2–4 and chemical modification of muscle fibres5. No clear conclusion has yet been reached. We have approached this question using an assay system in which sliding movements of fluorescently labelled single actin filaments along myosin filaments can be observed directly6,7. Here, we report direct measurement of the sliding of single actin filaments along one-headed myosin filaments in which the density of heads was varied over a wide range. Our results show that cooperative interaction between the two heads of myosin is not essential for inducing the sliding movement of actin filaments. More... »

PAGES

805-808

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/326805a0

DOI

http://dx.doi.org/10.1038/326805a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040356440

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3574452


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