Conformation, filament assembly, and activity of single-headed smooth muscle myosin

Journal of Biochemistry
K KonishiM Yazawa

Abstract

Single-headed myosin was prepared by digestion of porcine aorta smooth muscle myosin with Staphylococcus aureus V8 protease in the presence of actin. The single-headed myosin preparation contained intact light chains, a rod fragment of a heavy chain, and a heavy chain of which only a minor fraction contained a nick in the head segment. Below 0.2 M NaCl, the single-headed myosin showed a decrease in Ca2+-ATPase activity and an increase in the elution time on gel filtration HPLC in a phosphorylation-dependent manner, indicating a phosphorylation-dependent conformational transition between the extended and folded forms. These conformations were confirmed by electron microscopic observation of rotary-shadowed samples of single-headed myosin. However, the conformational transition of single-headed myosin occurred in a narrower range with lower salt concentrations than that of double-headed myosin. The filament assembly of single-headed myosin was thus facilitated and phosphorylation-independent. The single-headed myosin also showed high actin-activated ATPase activity independent of phosphorylation. These results indicate that the two-headed structure of smooth muscle myosin is not essential for the conformational transition, but is...Continue Reading

Citations

Nov 15, 2011·Journal of Molecular Biology·Bruce A J BaumannKenneth A Taylor
Nov 26, 2002·The Journal of Biological Chemistry·Jan L WahlstromChristine R Cremo
Jul 21, 2004·The Journal of Biological Chemistry·Sam M MazhariChristine R Cremo
Dec 5, 2002·The Journal of Biological Chemistry·Patricia A EllisonChristine R Cremo
Feb 20, 2021·The Journal of General Physiology·Lu WangChun Y Seow

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