Cravens Shannen L, Hobson Matthew, Stivers James T
Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine , 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States.
Biochemistry. 2014 Dec 9;53(48):7680-92. doi: 10.1021/bi501011m. Epub 2014 Nov 26.
Human uracil DNA glycosylase (hUNG) follows an extended reaction coordinate for locating rare uracil bases in genomic DNA. This process begins with diffusion-controlled engagement of undamaged DNA, followed by a damage search step in which the enzyme remains loosely associated with the DNA chain (translocation), and finally, a recognition step that allows the enzyme to efficiently bind and excise uracil when it is encountered. At each step along this coordinate, the enzyme must form DNA interactions that are highly specialized for either rapid damage searching or catalysis. Here we make extensive measurements of hUNG activity as a function of salt concentration to dissect the thermodynamic, kinetic, and electrostatic properties of key enzyme states along this reaction coordinate. We find that the interaction of hUNG with undamaged DNA is electrostatically driven at a physiological concentration of potassium ions (ΔGelect = -3.5 ± 0.5 kcal mol(-1)), with only a small nonelectrostatic contribution (ΔGnon = -2.0 ± 0.2 kcal mol(-1)). In contrast, the interaction with damaged DNA is dominated by the nonelectrostatic free energy term (ΔGnon = -7.2 ± 0.1 kcal mol(-1)), yet retains the nonspecific electrostatic contribution (ΔGelect = -2.3 ± 0.2 kcal mol(-1)). Stopped-flow kinetic experiments established that the salt sensitivity of damaged DNA binding originates from a reduction of kon, while koff is weakly dependent on salt. Similar findings were obtained from the salt dependences of the steady-state kinetic parameters, where the diffusion-controlled kcat/Km showed a salt dependence similar to kon, while kcat (limited by product release) was weakly dependent on salt. Finally, the salt dependence of translocation between two uracil sites separated by 20 bp in the same DNA chain was indistinguishable from that of kon. This result suggests that the transition-state for translocation over this spacing resembles that for DNA association from bulk solution and that hUNG escapes the DNA ion cloud during translocation. These findings provide key insights into how the ionic environment in cells influences the DNA damage search pathway.
人类尿嘧啶DNA糖基化酶(hUNG)在基因组DNA中定位稀有尿嘧啶碱基时遵循一个扩展的反应坐标。这个过程始于未受损DNA的扩散控制结合,接着是一个损伤搜索步骤,在此步骤中酶与DNA链保持松散结合(易位),最后是一个识别步骤,当遇到尿嘧啶时,该步骤允许酶有效地结合并切除尿嘧啶。沿着这个坐标的每一步,酶都必须形成高度专门化的DNA相互作用,以实现快速损伤搜索或催化。在这里,我们对hUNG活性作为盐浓度的函数进行了广泛测量,以剖析沿着这个反应坐标关键酶状态的热力学、动力学和静电性质。我们发现,在生理浓度的钾离子下,hUNG与未受损DNA的相互作用是由静电驱动的(ΔGelect = -3.5 ± 0.5 kcal mol(-1)),只有很小的非静电贡献(ΔGnon = -2.0 ± 0.2 kcal mol(-1))。相比之下,与受损DNA的相互作用则以非静电自由能项为主(ΔGnon = -7.2 ± 0.1 kcal mol(-1)),但仍保留非特异性静电贡献(ΔGelect = -2.3 ± 0.2 kcal mol(-1))。停流动力学实验表明,受损DNA结合的盐敏感性源于kon的降低,而koff对盐的依赖性较弱。从稳态动力学参数的盐依赖性也获得了类似的结果,其中扩散控制的kcat/Km表现出与kon相似的盐依赖性,而kcat(受产物释放限制)对盐的依赖性较弱。最后,在同一DNA链中被20个碱基对隔开的两个尿嘧啶位点之间易位的盐依赖性与kon的盐依赖性无法区分。这一结果表明,在这个间距上易位的过渡态类似于从本体溶液中DNA结合的过渡态,并且hUNG在易位过程中逃离了DNA离子云。这些发现为细胞中的离子环境如何影响DNA损伤搜索途径提供了关键见解。