Modeling H3 histone N-terminal tail and linker DNA interactions.
Molecular dynamics computer simulations were performed for the 25-residue N-terminal tail of the H3 histone protein in the proximity of a DNA segment of 10 base pairs (bp), representing a model for the linker DNA in chromatin. Several least biased configurations were used as initial configurations. The secondary structure content of the protein was increased by the presence of DNA close to it, but the locations of the secondary motifs were different for different initial orientations of the DNA grooves with respect to the protein. As a common feature to all simulations, the electrostatic attraction between negatively charged DNA and positively charged protein was screened by the water solvent and counterbalanced by the intrinsic compaction of the protein due to hydrophobic effects. The protein secondary structure limited the covering of DNA by the protein to 4-5 bp. The degree of compaction and charge density of the bound protein suggests a possible role of H3 tail in a nonspecific bending and plasticity of the linker DNA when the protein is located in the crowded dense chromatin.
La Penna
Giovanni
G
National Research Council, Institute for Macromolecular Studies, Via De Marini 6, 16149 Genova, Italy. lapenna@ge.ismac.cnr.it
Furlan
Sara
S
Perico
Angelo
A
D000595:Amino Acid Sequence; D020029:Base Pairing; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism; D003198:Computer Simulation; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017433:Protein Structure, Secondary; D055672:Static Electricity
D002843:Chromatin; D006657:Histones; D004247:DNA