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The myosin filament. XII. Effect of MgATP on assembly.

Authors
Type
Published Article
Journal
Journal of muscle research and cell motility
Publication Date
Volume
7
Issue
5
Pages
413–420
Identifiers
PMID: 3491833
Source
Medline
License
Unknown

Abstract

The effect of MgATP on myosin filament assembly has been studied. Filaments were assembled by a standard dilution procedure involving two steps, dilution from 0.6 to 0.3 M KCl and from 0.3 to 0.15 M KCl with a different rate of dilution in each step. This standard dilution procedure gives filaments which are structurally similar to native filaments in that they have a sharp length distribution around 1.5 micron, a diameter of 16 nm and they vary in length with KCl concentration in a similar manner to native filaments. The addition of 1 mM MgATP leads to a sharpening of the length distribution around 1.5 micron without change in the 16 nm diameter. Filaments assembled by dialysis or by rapid dilution are not similarly affected by the presence of MgATP indicating that the standard dilution procedure produces filaments which are more closely similar to native filaments than those produced by these other methods. MgAMPPNP and magnesium pyrophosphate have the same effect as MgATP thus eliminating the possibility that phosphorylation of the myosin is involved in the effect. The effect of MgATP is not directly related to its binding to the active site of the myosin molecule since a 500:1 mole ratio of MgATP to myosin is required for the effect. It is therefore likely that the effect of MgATP is related to other binding sites on the myosin molecule. The presence of MgATP leads to molecular rearrangements which finely tune the molecular organization of the filaments formed by the standard dilution procedure in vitro.(ABSTRACT TRUNCATED AT 250 WORDS)

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