Rotary DNA motors.
Many molecular motors move unidirectionally along a DNA strand powered by nucleotide hydrolysis. These motors are multimeric ATPases with more than one hydrolysis site. We present here a model for how these motors generate the requisite force to process along their DNA track. This novel mechanism for force generation is based on a fluctuating electrostatic 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 capsids. The motor can reverse its direction without reversing the polarity of its electrostatic field, that is, without major structural modifications of the protein. We also show that the motor can be driven by an ion gradient; thus the mechanism may apply as well to the bacterial flagellar motor and to ATP synthase.
Doering
C
C
Center for Nonlinear Studies, Los Alamos National Laboratory, New Mexico 87545, USA.
Ermentrout
B
B
Oster
G
G
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D017903:Bacteriophage T3 / Q000378:metabolism; D017123:Bacteriophage T7 / Q000201:enzymology; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004265:DNA Helicases / Q000737:chemistry / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008961:Models, Structural; D008962:Models, Theoretical; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
D004277:DNA, Single-Stranded; D014764:Viral Proteins; D004247:DNA; D000251:Adenosine Triphosphatases; D004265:DNA Helicases