Many molecular motors move unidirectionally along a DNA strand powered
by nucleotide hydrolysis. These motors are multimeric ATPases with mo
re than one hydrolysis site. We present here a model for how these mot
ors generate the requisite force to process along their DNA track. Thi
s novel mechanism for force generation is based on a fluctuating elect
rostatic field driven by nucleotide hydrolysis. We apply the principle
to explain the motion of certain DNA helicases and the portal protein
, the motor that bacteriophages use to pump the genome into their caps
ids. The motor can reverse its direction without reversing the polarit
y of its electrostatic field, that is, without major structural modifi
cations of the protein. We also show that the motor can be driven by a
n ion gradient; thus the mechanism may apply as well to the bacterial
flagellar motor and to ATP synthase.