Stepping behavior of two-headed kinesin motors

AbstractThe stepping behavior of the dimeric kinesin is studied by using our model based on previous biochemical, X-ray crystallography and cryo-electron microscopy studies. It is shown that, when a Pi is released from the trailing head, a forward step is made under a backward load smaller than the stall force; while when a Pi is released from the leading head, no stepping is made under a forward load or no load, and a backward step is made under a backward load. The forward stepping time, i.e., the time from the release of Pi in the trailing head to the binding of the ADP head to next binding site, is much smaller than the dwell time even under the backward load near the stall force. Thus the movement velocity of the kinesin dimer can be considered to be only dependent on ATPase rates of the two heads. The duration of the rising phase, i.e., the actual time taken by the ADP head to transit from the trailing to leading positions, is on the time scale of microseconds under any backward load smaller than the stall force. This is consistent with available experimental results

Mechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules

Kinesin molecules are motor proteins capable of moving along microtubule by hydrolyzing ATP. They generally have several forms of construct. This review focuses on two of the most studied forms: monomers such as KIF1A (kinesin-3 family) and dimers such as conventional kinesin (kinesin-1 family), both of which can move processively towards the microtubule plus end. There now exist numerous models that try to explain how the kinesin molecules convert the chemical energy of ATP hydrolysis into the mechanical energy to “power” their proceesive movement along microtubule. Here, we attempt to present a comprehensive review of these models. We further propose a new hybrid model for the dimeric kinesin by combining the existing models and provide a framework for future studies in this subject