Symmetry and Self-Assembly in Vertebrate A-Filaments

  • Arthur J. Rowe
  • Maria C. Maw
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)


The myosin-containing A-filaments of vertebrate skeletal muscle contain 294 myosin molecules packed to give overall 3-fold rotational symmetry, as illustrated by the fraying of the filament into 3 sub-filaments (Maw and Rowe, 1980). Further studies on slightly frayed filaments are consistent with a highly linear arrangement of these sub-filaments, at least in the major part of the cross-bridge region where sub-filaments can be observed. Isolated filaments have an unusual hydrodynamic property in the form of an anomalous frictional increment. This property is as yet unexplained; it may possibly be related to flow-induced cyclic movements in the myosin heads.

Self-assembly of A-filaments in vitro to correct length and width has yet to be achieved. We have found however that under certain exactly defined conditions a very accurate reconstruction of both filaments and A-band can be accomplished in situ. Solubilisation of the myosin in chloride-free medi­um and maintenance of a high local myosin concentration are absolute re­quirements. Reconstruction is either abolished or modified by pre­glycerolation or at longer sarcomere length. It is argued that these results suggest a role for the actin filament lattice in myosin assembly, and imply that myosin assembly in the M-line region may be separable from myosin assembly in the cross-bridge region.


Sarcomere Length Myosin Head Myosin Filament Myosin Molecule Rabbit Psoas 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Arthur J. Rowe
    • 1
  • Maria C. Maw
    • 1
  1. 1.Department of BiochemistryUniversity of LeicesterLeicesterUK

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