DNA-protein cooperative binding through variable-range elastic coupling.
Cooperativity plays an important role in the action of proteins bound to DNA. A simple mechanism for cooperativity, in the form of a tension-mediated interaction between proteins bound to DNA at two different locations, is proposed. These proteins are not in direct physical contact. DNA segments intercalating bound proteins are modeled as a worm-like chain, which is free to deform in two dimensions. The tension-controlled protein-protein interaction is the consequence of two effects produced by the protein binding. The first is the introduction of a bend in the host DNA and the second is the modification of the bending modulus of the DNA in the immediate vicinity of the bound protein. The interaction between two bound proteins may be either attractive or repulsive, depending on their relative orientation on the DNA. Applied tension controls both the strength and the range of protein-protein interactions in this model. Properties of the cooperative interaction are discussed, along with experimental implications.
Rudnick
J
J
Department of Physics, University of California at Los Angeles, Los Angeles, California 90095-1547, USA. jrudnick@physics.ucla.edu
Bruinsma
R
R
D055592:Biophysical Phenomena; D001703:Biophysics; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004548:Elasticity; D008954:Models, Biological; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
D011506:Proteins; D004247:DNA