Eliminating the First Inactive State and Stabilizing the Active State of the Cardiac Regulatory System Alters Behavior in Solution and in Ordered Systems.

ABSTRACT: Calcium binding to troponin C (TnC) is insufficient for full activation of myosin ATPase activity by actin-tropomyosin-troponin. Previous attempts to investigate full activation utilized ATP-free myosin or chemically modified myosin to stabilize the active state of regulated actin. We utilized the Δ14-TnT and the A8V-TnC mutants to stabilize the activated state at saturating Ca²⁺ and to eliminate one of the inactive states at low Ca²⁺. The observed effects differed in solution studies and in the more ordered in vitro motility assay and in skinned cardiac muscle preparations. At saturating Ca²⁺, full activation with Δ14-TnT·A8V-TnC decreased the apparent K_M for actin-activated ATPase activity compared to bare actin filaments. Rates of in vi

SUBMITTER: Johnson D 

PROVIDER: S-EPMC9396559 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature