Skip Residues and Charge Interactions in Myosin II Coiled-coils: Implications for Molecular Packing

• Published in: Journal of molecular biology Vol. 353; no. 3; pp. 613 - 628
• Main Authors: Straussman, Ravid, Squire, John M., Ben-Ya'acov, Ami, Ravid, Shoshana
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 28.10.2005
• Subjects: bipolar myosin filaments; coiled-coil skip residues; Fourier Analysis; Humans; Muscles; myosin filament structure; myosin II rod sequences; Myosin Type II - chemistry; Protein Conformation; Repetitive Sequences, Amino Acid; side-polar myosin filaments; Static Electricity; side-polar myosin filaments; MHC; bipolar myosin filaments; myosin filament structure; coiled-coil skip residues; myosin II rod sequences
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/j.jmb.2005.08.010

Molecular packing of myosin II coiled-coil rods into myosin filaments and the role of skip residues in the heptad sequence have been investigated. Sequence comparison of rods from skeletal, smooth and non-muscle myosin II shows that different myosin II subtypes have significantly different charge distributions. Analysis of the ionic interactions between adjacent rods with changing molecular overlap relates the different patterns of charge to the different structures of skeletal and smooth muscle myosin II filaments. It is shown in the case of skeletal muscle myosin II that the skip residues have a critical role in keeping these unique patterns of charge in perfect phase. Only one of the previously suggested packing models for myosin II filaments, with a slight modification, is supported, since it satisfies all the sequence-predicted axial shifts between adjacent rods. Such analysis significantly advances understanding of myosin filament assembly properties and will help to provide a basis for the proper understanding of myosin-associated diseases.