A model for processive movement of single-headed myosin-IX.
It is puzzling that in spite of its single-headed structure, myosin-IX can move processively along actin. Here, based on the experimental evidence that the strong binding of myosin to actin in rigor state induces structural changes to several local actin monomers, a Brownian ratchet model is proposed to describe this processive movement. In the model, the actin plays an active role in the motility of single-headed myosin, in contrast to the common belief that the actin acts only as a passive track for the motility of the myosin. The unidirectional movement is due to both the asymmetric periodic potential of the myosin interacting with actin and the forward Stokes force induced by the relative rotation of the neck domain to the motor domain, while the processivity is determined by the binding affinity of the myosin for actin in ATP state. This gives a good explanation to the high processivity of myosin-IX, which results from its high binding affinity for actin in ATP state due to the presence of unique loop 2 insertion or N-terminal extension. The experimental results on the motility of myosin-IX such as the step size, large forward/backward stepping ratio, run length, stall force, etc, are explained well.
Xie
Ping
P
Institute of Physics, Chinese Academy of Sciences, Beijing, China. pxie@aphy.iphy.ac.cn
D000199:Actins / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D000199:Actins; D000255:Adenosine Triphosphate; D009218:Myosins