Electron microscopy of negatively stained scallop myosin molecules. Effect of regulatory light chain removal on head structure.
The heads of myosin molecules from the striated adductor muscle of scallop have been studied by electron microscopy after negative staining. In common with vertebrate skeletal muscle myosin visualized by this method, the scallop myosin heads were pear-shaped and often showed pronounced curvature. Staining suggestive of two or, more frequently, three domains could often be observed. Removal of regulatory light chains (R-LCs) resulted in a reduction in the length of the heads of about 2.6 nm, with no significant change in maximum width. In desensitized preparations a majority of heads displayed anticlockwise curvature, whereas intact heads were usually seen curved clockwise. Analysis of the head curvature in both intact and desensitized molecules was consistent with an ability of each head to rotate about its long axis. Desensitization resulted in an increased incidence of heads showing two domains. It seems likely that the reduction in length upon removal of the R-LC is due to the two small domains located in the neck region of the head collapsing into one.
Walker
M
M
Muscle Biology Department, AFRC Institute of Food Research--Bristol Laboratory, Langford, U.K.
Trinick
J
J
D000818:Animals; D008854:Microscopy, Electron; D008974:Mollusca / Q000648:ultrastructure*; D009132:Muscles / Q000648:ultrastructure*; D015879:Myosin Subfragments; D009218:Myosins
D015879:Myosin Subfragments; D009218:Myosins