Modeling chain folding in protein-constrained circular DNA.
An efficient method for sampling equilibrium configurations of DNA chains binding one or more DNA-bending proteins is presented. The technique is applied to obtain the tertiary structures of minimal bending energy for a selection of dinucleosomal minichromosomes that differ in degree of protein-DNA interaction, protein spacing along the DNA chain contour, and ring size. The protein-bound portions of the DNA chains are represented by tight, left-handed supercoils of fixed geometry. The protein-free regions are modeled individually as elastic rods. For each random spatial arrangement of the two nucleosomes assumed during a stochastic search for the global minimum, the paths of the flexible connecting DNA segments are determined through a numerical solution of the equations of equilibrium for torsionally relaxed elastic rods. The minimal energy forms reveal how protein binding and spacing and plasmid size differentially affect folding and offer new insights into experimental minichromosome systems.
Martino
J A
JA
Department of Chemistry, Rutgers, The State University of New Jersey, Wright-Rieman Laboratories, Piscataway 08854, USA.
Olson
W K
WK
D001665:Binding Sites; D002875:Chromosomes; D004270:DNA, Circular / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004548:Elasticity; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D009010:Monte Carlo Method; D009690:Nucleic Acid Conformation; D009707:Nucleosomes; D013269:Stochastic Processes; D013314:Stress, Mechanical; D013816:Thermodynamics
D004270:DNA, Circular; D004268:DNA-Binding Proteins; D009707:Nucleosomes; D012321:DNA-Directed RNA Polymerases