A Cardiomyopathy Mutation in the Myosin Essential Light Chain Alters Actomyosin Structure.

ABSTRACT: We have used site-directed time-resolved fluorescence resonance energy transfer to determine the effect of a pathological mutation in the human ventricular essential light chain (hVELC) of myosin, on the structural dynamics of the actin-myosin complex. The hVELC modulates the function of actomyosin, through the interaction of its N-terminal extension with actin and its C-terminal lobe with the myosin heavy chain. Several mutations in hVELC are associated with hypertrophic cardiomyopathy (HCM). Some biochemical effects of these mutations are known, but further insight is needed about their effects on the structural dynamics of functioning actomyosin. Therefore, we introduced the HCM mutation E56G into a single-cysteine (C16) hVELC construct and substituted it for the VELC of bovine cardiac

SUBMITTER: Guhathakurta P 

PROVIDER: S-EPMC5510710 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature