Modification of the alkali light chains of skeletal myosin inhibits actin binding and adenosine triphosphate cleavage.
Heavy meromyosin treated with the ATP analog, 6,6'-dithiobis(inosinyl-5'-yl imidodiphosphate), (slppNHp)2, in the presence of adenyl-5'-yl imidodiphosphate at 0 degrees loses its EDTA-ATPase activity and actin binding ability in a parallel manner. Studies with myosin show that under the above conditions (slppNHp)2 reacts preferentially with the single cysteines of the alkali light chains (Mr = 20,700 and 16,500) suggesting a role for these subunits in regulating actin-myosin interaction and ATP cleavage.
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D015879:Myosin Subfragments / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D011485:Protein Binding; D011817:Rabbits
D000199:Actins; D046911:Macromolecular Substances; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins