Department of Chemistry, Johns Hopkins University , 3400 North Charles Street, Baltimore, Maryland 21218, United States.
Biochemistry. 2013 Sep 17;52(37):6301-3. doi: 10.1021/bi400997h. Epub 2013 Sep 9.
Translesion synthesis past an oxidized abasic site, 2-deoxyribonolactone, in Escherichia coli results in high levels of dG incorporation and is dependent upon DNA polymerase V (Pol V). Kinetic experiments performed here affirm that Pol V preferentially incorporates dG opposite 2-deoxyribonolactone (L). Pol V discriminates between dG and dA on the basis of the apparent KD, suggesting that L provides instructive structural information to the enzyme despite lacking a Watson-Crick base.
跨损伤合成越过氧化的碱基缺失部位 2-脱氧核糖酮内酯在大肠杆菌中导致高水平的 dG 掺入,并且依赖于 DNA 聚合酶 V(Pol V)。此处进行的动力学实验证实,Pol V 优先将 dG 掺入到 2-脱氧核糖酮内酯(L)的对面。Pol V 根据表观 KD 值区分 dG 和 dA,表明尽管 L 缺乏 Watson-Crick 碱基,但它为酶提供了有指导意义的结构信息。