Thermodynamic origin of cooperativity in actomyosin interactions: The coupling of short-range interactions with actin bending stiffness in an Ising-like model

Author(s)

Alencar, Adriano M. ^{[1, 2]} ; Butler, James P. ^{[2, 3]} ; Mijailovich, Srboljub M. ^[2]

Affiliation

^[1] Univ Sao Paulo, Dept Pathol, Sch Med, BR-01246903 Sao Paulo - Brazil

^[2] Harvard Univ, Dept Environm Hlth, Sch Publ Hlth, Boston, MA 02115 - USA

^[3] Harvard Univ, Dept Med, Sch Med, Boston, MA 02115 - USA

• Document type: Journal article
• Source: Physical Review E; v. 79, n. 4, p. 041906, 2009.
• Web of Science Citations: 5

Abstract

We present Monte Carlo simulations for a molecular motor system found in virtually all eukaryotic cells, the acto-myosin motor system, composed of a group of organic macromolecules. Cell motors were mapped to an Ising-like model, where the interaction field is transmitted through a tropomyosin polymer chain. The presence of Ca2+ induces tropomyosin to block or unblock binding sites of the myosin motor leading to its activation or deactivation. We used the Metropolis algorithm to find the transient and the equilibrium states of the acto-myosin system composed of solvent, actin, tropomyosin, troponin, Ca2+, and myosin-S1 at a given temperature, including the spatial configuration of tropomyosin on the actin filament surface. Our model describes the short- and long-range cooperativity during actin-myosin binding which emerges from the bending stiffness of the tropomyosin complex. We found all transition rates between the states only using the interaction energy of the constituents. The agreement between our model and experimental data also supports the recent theory of flexible tropomyosin. (AU)