Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.

ABSTRACT: The β-myosin heavy chain expressed in ventricular myocardium and the myosin heavy chain (MyHC) in slow-twitch skeletal Musculus soleus (M. soleus) type-I fibers are both encoded by MYH7. Thus, these myosin molecules are deemed equivalent. However, some reports suggested variations in the light chain composition between M. soleus and ventricular myosin, which could influence functional parameters, such as maximum velocity of shortening. To test for functional differences of the actin gliding velocity on immobilized myosin molecules, we made use of in vitro motility assays. We found that ventricular myosin moved actin filaments with ∼0.9 µm/s significantly faster than M. soleus myosin (0.3 µm/s). Filaments prepared from isolated actin are not the native interaction partner of myosin and are

SUBMITTER: Osten J 

PROVIDER: S-EPMC9441736 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature