Myosin filament assembly requires a cluster of four positive residues located in the rod domain

摘要

Myosin has an intrinsic ability to organize into ordered thick filaments that mediate muscle contraction. Here, we use surface plasmon resonance and light scattering analysis to further characterize the molecular determinants that guide myosin filament assembly. Both assays identify a cluster of lysine and arginine residues as important for myosin polymerization in vitro. Moreover, in cardiomyocytes, replacement of these charged residues by alanine severely affects the incorporation of myosin into the distal ends of the sarcomere. Our findings show that a novel assembly element with a distinct charge profile is present at the C-terminus of sarcomeric myosins. Structured summary of protein interactions: WT LMM binds to WT LMM by surface plasmon resonance (View Interaction) WT LMM binds to CT2 LMM by surface plasmon resonance (View Interaction) WT LMM binds to Alanine mutant LMM by surface plasmon resonance (View Interaction) WT LMM and WT LMM bind by light scattering (View Interaction) Alanine mutant LMM and Alanine mutant LMM bind by light scattering (View Interaction) WT LMM and Alanine mutant LMM bind by light scattering (View Interaction).