ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) |
a molecular mechanical model for the Kar3/Vik1 heterodimer is described based on structural, kinetic and motility data revealing a long-range chemomechanical transmission mechanism that resembles a familiar fishing tactic. By this this molecular fishing, ATP-binding to Kar3 dissociates catalytically inactive Vik1 off microtubule to facilitate minus-end sliding of the dimer on the microtubule lattice. When the dimer binds the frayed ends of the microtubules, the fishing channels ATP hydrolysis energy into the microtubule depolymerization by a mechanochemical effect |
Saccharomyces cerevisiae |
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