Department of Biochemistry and Molecular Biology and the UF-Shands Cancer Center, University of Florida College of Medicine, Gainesville, FL 32610, USA.
DNA Repair (Amst). 2012 Dec 1;11(12):951-64. doi: 10.1016/j.dnarep.2012.09.004. Epub 2012 Oct 11.
S(N)1 DNA methylating agents are genotoxic agents that methylate numerous nucleophilic centers within DNA including the O(6) position of guanine (O(6)meG). Methylation of this extracyclic oxygen forces mispairing with thymine during DNA replication. The mismatch repair (MMR) system recognizes these O(6)meG:T mispairs and is required to activate DNA damage response (DDR). Exonuclease I (EXO1) is a key component of MMR by resecting the damaged strand; however, whether EXO1 is required to activate MMR-dependent DDR remains unknown. Here we show that knockdown of the mouse ortholog (mExo1) in mouse embryonic fibroblasts (MEFs) results in decreased G2/M checkpoint response, limited effects on cell proliferation, and increased cell viability following exposure to the S(N)1 methylating agent N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), establishing a phenotype paralleling MMR deficiency. MNNG treatment induced formation of γ-H2AX foci with which EXO1 co-localized in MEFs, but mExo1-depleted MEFs displayed a significant diminishment of γ-H2AX foci formation. mExo1 depletion also reduced MSH2 association with DNA duplexes containing G:T mismatches in vitro, decreased MSH2 association with alkylated chromatin in vivo, and abrogated MNNG-induced MSH2/CHK1 interaction. To determine if nuclease activity is required to activate DDR we stably overexpressed a nuclease defective form of human EXO1 (hEXO1) in mExo1-depleted MEFs. These experiments indicated that expression of wildtype and catalytically null hEXO1 was able to restore normal response to MNNG. This study indicates that EXO1 is required to activate MMR-dependent DDR in response to S(N)1 methylating agents; however, this function of EXO1 is independent of its nucleolytic activity.
S(N)1 型 DNA 甲基化试剂是一种遗传毒性试剂,可使 DNA 中的许多亲核中心甲基化,包括鸟嘌呤的 O(6)位(O(6)meG)。这种环外氧的甲基化迫使 DNA 复制过程中胸腺嘧啶错配。错配修复(MMR)系统识别这些 O(6)meG:T 错配,并激活 DNA 损伤反应(DDR)。核酸外切酶 I(EXO1)是 MMR 的关键组成部分,通过切除受损链;然而,EXO1 是否需要激活 MMR 依赖性 DDR 尚不清楚。在这里,我们发现在小鼠胚胎成纤维细胞(MEFs)中敲低其同源物(mExo1)会导致 G2/M 检查点反应减弱,对细胞增殖的影响有限,并且在用 S(N)1 甲基化试剂 N-甲基-N'-硝基-N-亚硝基胍(MNNG)处理后细胞活力增加,这建立了与 MMR 缺陷相似的表型。MNNG 处理诱导 γ-H2AX 焦点的形成,EXO1 与 MEFs 中的焦点共定位,但 mExo1 耗尽的 MEFs 显示出 γ-H2AX 焦点形成的显着减少。mExo1 耗尽还减少了 MSH2 与体外含有 G:T 错配的 DNA 双链体的结合,减少了 MSH2 与体内烷基化染色质的结合,并消除了 MNNG 诱导的 MSH2/CHK1 相互作用。为了确定核酸酶活性是否需要激活 DDR,我们在 mExo1 耗尽的 MEFs 中稳定过表达了人类 EXO1(hEXO1)的核酸酶缺陷形式。这些实验表明,野生型和催化无效型 hEXO1 的表达能够恢复对 MNNG 的正常反应。这项研究表明,EXO1 是激活 S(N)1 甲基化试剂诱导的 MMR 依赖性 DDR 所必需的;然而,EXO1 的此功能独立于其核酸酶活性。