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M108793200v1
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Papers In Press, published online ahead of print February 25, 2002
J. Biol. Chem, 10.1074/jbc.M108793200
Submitted on September 12, 2001
Revised on January 10, 2002
Accepted on February 22, 2002

The role of ATP hydrolysis for kinesin processivity

Christopher M. Farrell, Andrew T. Mackey, Lisa M. Klumpp, and Susan P. Gilbert

Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260

Corresponding Author: spg1{at}pitt.edu

Conventional kinesin is a highly processive, plus-end directed microtubule-based motor that drives membranous organelles toward the synapse in neurons. Although recent structural, biochemical, and mechanical measurements are beginning to converge into a common view of how kinesin converts the energy from ATP turnover into motion, it remains difficult to dissect experimentally the intermolecular domain cooperativity required for kinesin processivity. We report here our pre-steady-state kinetic analysis of a kinesin switch I mutant at Arg210 (NxxSSRSH, residues 205-212 in Drosophila kinesin). The results show that the R210A substitution results in a dimeric kinesin that is defective for ATP hydrolysis and a motor that cannot detach from the microtubule even though ATP binding and microtubule association occur. We propose a mechanistic model in which ATP binding at head 1 leads to the plus-end directed motion of the neck linker to position head 2 forward at the next microtubule binding site. However, ATP hydrolysis is required at head 1 to lock head 2 onto the microtubule in a tight binding state before head 1 dissociation from the microtubule. This mechanism optimizes forward movement and processivity by ensuring that one motor domain is tightly bound to the microtubule before the second can detach.


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