The myosin filament. XIII. The sensitivity of LMM assembly to Mg.ATP.
An LMM fragment (Mr 62,000) of myosin has been prepared which has aggregation properties that are sensitive to the presence of Mg.ATP. Aggregation of the LMM by reducing the ionic strength in the presence of 1 mM Mg.ATP produces non-periodic aggregates which gradually rearrange to paracrystals with a 43 nm axial repeat pattern. This fragment includes the C-terminal end of the myosin rod starting at residue 1376. Therefore, at least one of the Mg.ATP binding sites responsible for this effect is located somewhere along this region of the myosin rod. Although assembly of the rod fragment of myosin into paracrystals does not show sensitivity to Mg.ATP, assembly of intact myosin molecules to form filaments does show sensitivity to Mg.ATP. For myosin filaments, assembly initially gives a broad distribution around a mean length of 1.5 microns, which sharpens around the mean length with time. The rearrangement of the LMM rods and intact myosin molecules both induced by the presence of Mg.ATP are probably related. These findings highlight the complexity of the cooperative interactions between different portions of the myosin molecule that are involved in determining the assembly properties of the intact molecule.
Chowrashi
P K
PK
Department of Anatomy, School of Medicine, University of Pennsylvania, Philadelphia 19104-6058.
Pepe
F A
FA
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism*; D008854:Microscopy, Electron; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D011817:Rabbits
D000255:Adenosine Triphosphate; D009218:Myosins