Dinitrophenylation of phosphorylated gizzard myosin. Labelling of the subfragment 1 region.

ABSTRACT

Chymotrypsin and papain digestion of 3H-labelled dinitrophenylated chicken gizzard myosin, pretreated with the myosin light chain catalyzed phosphorylating system, released a subfragment 1 devoid of its light chains but containing all of the label associated with the thiols of the heavy chain region. This was also the case when myosin was incubated in the presence of the phosphorylating system but without ATP. Dinitrophenylation of a reconstituted actomyosin made from phosphorylated myosin occurred mainly on -SH groups of the heavy chains, in contrast to the predominant modification of the light chains of myosin from a control actomyosin that was treated similarly. Conformational changes in myosin may govern, in part, actin-myosin interaction through the phosphorylation of the light chain of Mr 20.000.