UNAM-National Nanotechnology Research Center and Institute of Materials Science & Nanotechnology, Bilkent University, Ankara 06800, Turkey.
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA; Department of Physics & Astronomy, Northwestern University, Evanston, IL 60208, USA.
Curr Opin Chem Biol. 2019 Dec;53:118-124. doi: 10.1016/j.cbpa.2019.08.007. Epub 2019 Oct 2.
Dissociation of a protein from DNA is often assumed to be described by an off rate that is independent of other molecules in solution. Recent experiments and computational analyses have challenged this view by showing that unbinding rates (residence times) of DNA-bound proteins can depend on concentrations of nearby molecules that are competing for binding. This 'facilitated dissociation' (FD) process can occur at the single-binding site level via formation of a ternary complex, and can dominate over 'spontaneous dissociation' at low (submicromolar) concentrations. In the crowded intracellular environment FD introduces new regulatory possibilities at the level of individual biomolecule interactions.
蛋白质从 DNA 上的解离通常被认为可以用独立于溶液中其他分子的解吸速率来描述。最近的实验和计算分析通过显示 DNA 结合蛋白的解吸速率（停留时间）可以依赖于竞争结合的附近分子的浓度，对这一观点提出了挑战。这种“促进解离”（FD）过程可以通过形成三元复合物在单个结合位点水平上发生，并且可以在低（亚微摩尔）浓度下主导“自发解离”。在拥挤的细胞内环境中，FD 在单个生物分子相互作用的水平上引入了新的调控可能性。
