Literature DB >> 2674720

Bidirectional movement of actin filaments along tracks of myosin heads.

Y Y Toyoshima1, C Toyoshima, J A Spudich.   

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.

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Year:  1989        PMID: 2674720     DOI: 10.1038/341154a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  23 in total

1.  Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties.

Authors:  T Nishizaka; R Seo; H Tadakuma; K Kinosita; S Ishiwata
Journal:  Biophys J       Date:  2000-08       Impact factor: 4.033

2.  On the mechanics of the actin filament: the linear relationship between stiffness and yield strength allows estimation of the yield strength of thin filament in vivo.

Authors:  Enrico Grazi; Orietta Cintio; Giorgio Trombetta
Journal:  J Muscle Res Cell Motil       Date:  2004       Impact factor: 2.698

Review 3.  Myosin step size: estimates from motility assays and shortening muscle.

Authors:  K Burton
Journal:  J Muscle Res Cell Motil       Date:  1992-12       Impact factor: 2.698

4.  The yeast type II myosin heavy chain: analysis of its predicted polypeptide sequence.

Authors:  F P Sweeney; M J Pocklington; E Orr
Journal:  J Muscle Res Cell Motil       Date:  1991-02       Impact factor: 2.698

5.  Diffusion of heavy meromyosin in the presence of F-actin and ATP.

Authors:  J Borejdo; S Burlacu
Journal:  J Muscle Res Cell Motil       Date:  1992-02       Impact factor: 2.698

6.  Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis.

Authors:  Masaaki K Sato; Takashi Ishihara; Hiroto Tanaka; Akihiko Ishijima; Yuichi Inoue
Journal:  Biophys J       Date:  2012-08-22       Impact factor: 4.033

Review 7.  The mechanics of force generation by kinesin.

Authors:  J Howard
Journal:  Biophys J       Date:  1995-04       Impact factor: 4.033

8.  Kinesin swivels to permit microtubule movement in any direction.

Authors:  A J Hunt; J Howard
Journal:  Proc Natl Acad Sci U S A       Date:  1993-12-15       Impact factor: 11.205

9.  Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap.

Authors:  K Saito; T Aoki; T Aoki; T Yanagida
Journal:  Biophys J       Date:  1994-03       Impact factor: 4.033

10.  Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit.

Authors:  Vijay S Rao; Ellisha N Marongelli; William H Guilford
Journal:  Cell Motil Cytoskeleton       Date:  2009-01
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