Chemistry Letters, Vol.41, No.9, 874-876, 2012
Histone-like Protein HCcp3-induced Liquid Crystalline DNA Condensation
From prokaryotes to eukaryotes, the DNA condensation process by basic proteins is essential to store the genome in vivo. The surface charge inversion with a DNA/HCcp3 charge ratio of 0.7/1 indicates a role for HCcp3-mediated counter ion-driven mechanism in DNA condensation. The formation of the cholesteric liquid-crystalline phase of DNA HCcp3 complexes occurred when DNA charges were neutralized. The results suggest that DNA condensation processes by HCcp3 can be divided into two distinctive binding stages: the first state, prior to condensation, involves an entropy-driven binding process of HCcp3 to the DNA, while the second state is an electrostatically driven condensing and assembling process.