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PMID: 2674720 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Bidirectional movement of actin filaments along tracks of myosin heads.

Nature ·Vol. 341 ·No. 6238 ·1989-09-14 ·Pages 154-6

Toyoshima YY, Toyoshima C, Spudich JA

Abstract

It is well established that muscle contraction results from the relative sliding of actin and myosin filaments. Both filaments have definite polarities and well-ordered structures. Thick filaments, however, are not vital for supporting movement in vitro. Previously we have demonstrated that actin filaments can move continuously on myosin fragments (subfragment-1 or heavy meromyosin (HMM] that are bound to a nitrocellulose surface. Here we report that actin filaments can move in opposite directions on tracks of myosin heads formed when actin filaments decorated with HMM are placed on a nitrocellulose surface. The actin filaments always move forward, frequently changing the direction of the movement, but never move backward reversing the polarity of the movement. The direction of movement is therefore determined by the polarity of the actin filament. These results indicate that myosin heads have considerable flexibility.

MeSH Terms
Actins/metabolism,ultrastructure Adenosine Triphosphate/metabolism Fluorescent Antibody Technique Microscopy, Electron Myosin Subfragments/metabolism Myosins/metabolism,ultrastructure Peptide Fragments/metabolism
Chemicals
Actins Myosin Subfragments Peptide Fragments Adenosine Triphosphate Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Toyoshima Y Y
Department of Cell Biology, Stanford University School of Medicine, California 94305.
Toyoshima C
Spudich J A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1989-09-14
Pages
154-6
Language
English
Region
England
NLM ID
0410462
Subset
IM
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