人类 8-氧鸟嘌呤糖基化酶 OGG1 通过半胱氨酸和组氨酸的加成作用裂解消融位点并与 3'-DNA 端部共价结合。

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS
Cameron Bryan, Kun Yang
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引用次数: 0

摘要

8-氧代鸟嘌呤糖基化酶 1(OGG1)可修复主要的 DNA 氧化损伤--8-氧代-2'-脱氧鸟苷。据报道,OGG1 能切开最常见的 DNA 损伤--嘌呤/近嘧啶(AP)位点,并在此过程中形成稳定的 DNA-OGG1 交联。然而,这种加合物的化学结构并不确定。在这里,我们报告说,DNA-OGG1 交联是由半胱氨酸和组氨酸加到 3'-DNA 端部切口 AP 位点上形成的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Human 8-Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3'-DNA Termini via Cysteine and Histidine Addition.

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.

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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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