An overview of protein-DNA and protein-RNA interactions

Abstract

In this review the fundamental question of how does protein-DNA or protein-RNA interactions affect the structures and dynamics of DNA, RNA, and protein is addressed. Two models of human serum albumin (HSA) bindings to calf-thymus DNA and transfer RNA (tRNA) are presented here. In these models the binding sites, stability and structural aspects of DNA-protein and RNA-protein are discussed. Electrostatic binding of DNA or RNA via backbone phosphate group to the positively charged amino acids on the surface of protein is prevailing. Two binding sites with K₁ = 4.8 × 10⁵ M⁻¹ and K₂ = 6.1 × 10⁴ M⁻¹ for protein-DNA and one binding affinity with K = 1.45 × 10⁴ M⁻¹ for protein-RNA are observed. A partial B to A-DNA transition is observed for protein-DNA complexes, while tRNA remains in A-family structure upon protein interaction.