title: Capping one end of an actin filament affects elongation at the other end.
abstract: The rates of elongation at the free ends of actin filaments were compared to those of intact filaments, when the one end was masked with muscle beta-actinin or cytochalasin D, using fixed actoheavy meromyosin and Limulus acrosomal actin bundles as seeds. Experimental conditions were chosen so as to prevent spontaneous filament formation as far as possible. The rate of elongation at the barbed end of fixed actoheavy meromyosin was reduced to about one-fourth when the other pointed end was capped by beta-actinin, and that at the pointed end was reduced to one-third when the barbed end was blocked by cytochalasin D. Similar effects were also observed with the packed actin bundles of horseshoe crab sperm, although the decreases in elongation were less marked: 50-60% of the control both in the presence of beta-actinin and cytochalasin D. To explain the peculiar "end effect" described above, it is proposed that possible conformational changes at one end of an actin filament caused by the binding of a capping substance are transmitted successively to the other end so as to affect the elongation there.
mesh_terms: D000185:Actinin / Q000502:physiology*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D015638:Cytochalasin D; D003572:Cytochalasins / Q000494:pharmacology*; D006737:Horseshoe Crabs; D007700:Kinetics; D008854:Microscopy, Electron; D009132:Muscles / Q000648:ultrastructure; D009210:Myofibrils / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure*; D015879:Myosin Subfragments / Q000502:physiology; D011817:Rabbits
chemical_list: D000199:Actins; D003572:Cytochalasins; D015879:Myosin Subfragments; D000185:Actinin; D015638:Cytochalasin D