The DNA of human cells suffers about 1.000-100.000 oxidative lesions per day. One of the most common defects in this category is represented by 7,8-dihydro-8-oxoguanine. There are numerous exogenous effects on DNA that induce the intracellular generation of 7, 8-dihydro-8-oxoguanine. Therefore, a quantitatively sufficient repair of all occurring oxidative damaged guanine bases is often only partially feasible, especially in advanced age. Inadequate removal of these damages can subsequently lead to mutations and thus to serious diseases. All these aspects represent a dangerous situation for an organism. However, it is suspected that the amount of the 8-oxoguanine DNA glycosylase can be actively regulated on the level of gene expression by the redox-active properties of ubiquinol and thus its protein expression can be controlled. Using an real-time base excision repair assay including a melting curve analysis, the activity of the human 8-oxoguanine DNA glycosylase 1 was measured under the influence of ubiquinol. It was possible to observe a concentration-dependent increase in the activity of the 8-oxoguanine DNA glycosylase 1 under the influence of ubiquinol for the first time, both on purified and commercially acquired enzyme as well as on enzyme isolated from mitochondria of human fibroblasts. An increase in activity of this enzyme based on a change in cellular redox state caused by ubiquinol could not be confirmed. In addition, an increased gene expression of 8-oxoguanine-DNA glycosylase 1 under ubiquinol could not be observed. However, there was a change in bifunctionality in favor of an increased N-glycosylase activity and a direct interaction between ubiquinol and 8-oxoguanine DNA glycosylase 1. We suggest that ubiquinol contributes to the dissolution of a human 8-oxoguanine DNA glycosylase 1 end-product complex that forms after cutting into the sugar-phosphate backbone of the DNA with the resulting unsaturated 3'-phospho-α, β-aldehyde end and thereby inhibits further enzymatic steps.

中文翻译：

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DNA修复酶hOGG1的活性可以被泛醇直接调节。

人体细胞的DNA每天遭受约1.000-100.000氧化损伤。该类别中最常见的缺陷之一是7,8-二氢-8-氧鸟嘌呤。对DNA有许多外源效应，可诱导细胞内生成7、8-二氢-8-氧鸟嘌呤。因此，对所有发生的氧化损伤的鸟嘌呤碱基进行定量上充分的修复通常仅是部分可行的，尤其是在老年期。这些损害的清除不充分会导致突变，从而导致严重的疾病。所有这些方面都代表了生物体的危险情况。然而，怀疑通过泛醇的氧化还原活性，可以在基因表达水平上主动调节8-氧鸟嘌呤DNA糖基化酶的量，从而可以控制其蛋白质表达。使用包括熔解曲线分析的实时碱基切除修复测定法，在泛醇的影响下测量了人8-氧鸟嘌呤DNA糖基化酶1的活性。首次观察到在泛醇的作用下，对8-氧鸟嘌呤DNA糖基化酶1活性的浓度依赖性增加，这既对纯化的和商业获得的酶，又对从人成纤维细胞的线粒体分离的酶都有影响。由于泛醇引起的细胞氧化还原状态的改变，无法确认该酶的活性增加。另外，未观察到在泛醇下8-氧鸟嘌呤-DNA糖基化酶1的基因表达增加。然而，