Functional significance of the binding of one myosin head to two actin monomers

Biochemistry
K Lheureux, P Chaussepied

Abstract

The functional significance of the interaction of one myosin head (S1) with two actin monomers was investigated by comparing the properties of the cross-linked monomeric and filamentous actin-S1 complexes. S1 was cross-linked to monomeric actin (G-actin) either in the absence or in the presence of DNase I by 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide. The binary G-actin-S1 and ternary DNase I-G-actin-S1 complexes were then purified by a combination of ion exchange and gel filtration columns. Both the binary and the ternary complexes were characterized by negligible, though different, Mg(2+)-ATPase activities of 0.018 and 0.006 s-1s(-1), respectively. Using fluorescence, light-scattering, and ultracentrifugation experiments, we found that only the binary G-actin-S1 complex could be polymerized in the presence of 2 mM MgCl2. Electron microscopic analysis of the cross-linked filamentous complex showed fully decorated filaments with the arrowhead pattern characteristic of the non-covalent complex in the rigor state. Such a 100% cross-linked F-actin-S1 complex exhibited a Mg(2+)-ATPase activity of 6.2 +/- 0.8 s-1, slightly lower than the maximum velocity of the non-cross-linked complex of 8.6 +/- 0.8 s-1, but comparable to the ...Continue Reading

Citations

Dec 10, 2002·Biochemical and Biophysical Research Communications·Keiichi YokoyamaMakoto Suzuki
Jan 7, 2000·Journal of Molecular Biology·C SmyczynskiP Chaussepied

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