The transmission of stability or instability from site specific protein-DNA complexes.
Theoretical calculations were made to determine the influence of side specific 'melting' and 'stabilizing' proteins on the thermal stability of nearby base pairs (bp). A DNA sequence 999bp. long containing the 123 bp. lactose operon control region in the center was examined. Melting curves of base pairs near the binding sites of the catabolite activator protein, CAP, the lactose repressor, and RNA polymerase were calculated in the absence and presence of each protein. The empirical loop entropy model of the helix-coil transition of DNA was employed. Calculations show that melting and stabilizing proteins alter the tm of base pairs 20 to 100 bp-away. The magnitude and range of the effect is strongly influenced by the base pair composition and sequence of the protein site and the immediately adjacent DNA regions.
D001665:Binding Sites; D004247:DNA; D012321:DNA-Directed RNA Polymerases; D004355:Drug Stability; D007785:Lactose / Q000378:metabolism; D046911:Macromolecular Substances; D008433:Mathematics; D008970:Molecular Weight; D009691:Nucleic Acid Denaturation; D009876:Operon; D011485:Protein Binding; D011506:Proteins; D012333:RNA, Messenger; D013696:Temperature
D046911:Macromolecular Substances; D011506:Proteins; D012333:RNA, Messenger; D004247:DNA; D012321:DNA-Directed RNA Polymerases; D007785:Lactose