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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)

Abstract

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.

Keywords

Sarcomere Length Myosin Head Myosin Filament Myosin Molecule Rabbit Psoas 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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