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- W2792109596 abstract "We expressed and studied the motor domain of human β-cardiac myosin carrying one of 5 Dilated CardioMyopathy (DCM) mutations in mouse C2C12 cells. Using the purified protein we completed a biochemical kinetic analysis of the individual events in the ATPase cycle. This revealedl that each mutation alters different steps in the cycle depending upon its location in the motor domain. For example different mutation have enhanced or reduced ATP, ADP or actin affinity, enhanced or reduced rate constants of ATP binding, ATP hydrolysis or ADP release. Thus local effects dominate with no common pattern for the changes observed that could account for the similar clinical phenotype resulting from each mutation. Nor is there a distinct set of changes that distinguish DCM mutations from the Hypertrophic CardioMyopathy (HCM) mutations we have previously analysed. However when using the data for each step in the cycle to model the complete ATPase contraction cycle some themes emerge. All DCM linked mutations result in a lower duty ratio due to reduced occupancy of the force holding, AM.ADP complex in the steady-state. Under load the AM.ADP complex is predicted to increase due to a reduced rate constant for ADP release, and this effect is blunted for each DCM mutation. These results predict that sarcomeres expressing myosin with DCM mutations would have impaired force generation & force holding capacity and a lower efficiency of ATP usage compared to wild type protein. This result is the opposite of that we reported recently for a HCM mutation, R453C (Mijailovich et al 2017 Biophys J 112: 984-996) and the same is shoiwn here for the R403Q HCM linked mutation. Grant: NIH-R01 GM29090" @default.
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- W2792109596 date "2018-02-01" @default.
- W2792109596 modified "2023-10-14" @default.
- W2792109596 title "ATPase Cycle Analysis Predicts that Mutations Linked to Dilated Cardiomyopathy in Human Beta Myosin Will Impair Force Generation" @default.
- W2792109596 doi "https://doi.org/10.1016/j.bpj.2017.11.1178" @default.
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