Kinetic analysis of the nucleic acid chaperone activity of the Hepatitis C virus core protein

摘要: The multifunctional HCV core protein consists of a hydrophilic RNA interacting D1 domain and hydrophobic D2 with membranes lipid droplets. was found to possess nucleic acid annealing strand transfer properties. To further understand these chaperone properties, we investigated how the two peptides encompassing basic clusters chaperoned complementary canonical acids that correspond DNA sequences HIV-1 transactivation response element TAR its cTAR. were augment cTAR-dTAR kinetics by at least three orders magnitude. rate not affected modifications dTAR loop but strongly reduced stabilization cTAR stem ends, suggesting core-directed reaction is initiated through terminal bases dTAR. Two kinetic pathways identified fast pre-equilibrium intermediate then slowly converts into final extended duplex. slow differed number base pairs, which should be melted nucleate intermediates. operate similarly, confirming properties are mostly supported clusters.