人类8-氧代鸟嘌呤糖基化酶OGG1切割无碱基位点并通过添加半胱氨酸和组氨酸与3'-DNA末端共价结合。
Human 8-Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3'-DNA Termini via Cysteine and Histidine Addition.
作者信息
Bryan Cameron, Yang Kun
机构信息
Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy, The University of Texas at Austin, Austin, Texas, 78712, United States.
出版信息
Chembiochem. 2025 Jan 14;26(2):e202400705. doi: 10.1002/cbic.202400705. Epub 2024 Nov 11.
Abstract
8-Oxoguanine glycosylase 1 (OGG1) repairs the major oxidative DNA damage, 8-oxo-2'-deoxyguanosine. It has been reported that OGG1 incises the most frequently formed DNA lesion, apurinic/apyrimidinic (AP) site, and in the process a stable DNA-OGG1 cross-link is formed. However, the chemical structure of the adduct is not characterized. Here, we report that DNA-OGG1 cross-links result from cysteine and histidine addition to incised AP sites at 3'-DNA termini.
摘要
8-氧代鸟嘌呤糖基化酶1（OGG1）修复主要的氧化性DNA损伤——8-氧代-2'-脱氧鸟苷。据报道，OGG1能切割最常见形成的DNA损伤——无嘌呤/无嘧啶（AP）位点，并且在此过程中会形成稳定的DNA-OGG1交联。然而，该加合物的化学结构尚未得到表征。在此，我们报告DNA-OGG1交联是由半胱氨酸和组氨酸添加到3'-DNA末端切割后的AP位点所导致的。
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