Parking problem and negative cooperativity of binding of myosin subfragment 1 to F-actin
Date of Original Version
Previously we provided evidence that myosin subfragment 1 (S1) can bind either one (state 1) or two actin monomers (state 2) in solution and in muscle fiber. Here we present results of the kinetics study of binding of S1 to F-actin labeled with fluorescent dye pyrene. A transition from state 1 to state 2 depends on probability that the second actin is free, which is high when molar ratio of S1/actin (R) is less than 0.5, and it decreases dramatically when R>2.0 due to the parking problem. The kinetics data obtained at different molar ratios were well fitted by two binding states model. The sequential binding of myosin head initially with one actin monomer and then with the second actin monomer in F-actin can play a key role in force generation by actin-myosin and their directed movement. © 2012 Elsevier Inc.
Publication Title, e.g., Journal
Biochemical and Biophysical Research Communications
Reshetnyak, Yana K., Cynthia N. Prudence, James Segala, Vladislav S. Markin, and Oleg A. Andreev. "Parking problem and negative cooperativity of binding of myosin subfragment 1 to F-actin." Biochemical and Biophysical Research Communications 425, 4 (2012): 746-749. doi: 10.1016/j.bbrc.2012.07.146.