Work

Human 8‐Oxoguanine Glycosylase OGG1 Cleaves Abasic Sites and Covalently Conjugates to 3′‐DNA Termini via Cysteine and Histidine Addition

Year: 2024

Type: article

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.

Source: ChemBioChem

DOI: 10.1002/cbic.202400705

Authors: Cameron Bryan, Kun Yang

Institution: The University of Texas at Austin

Language: English

Topic: DNA Repair Mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Harvey Mudd College, University of Texas at Austin, National Institutes of Health, National Institute of General Medical Sciences

Award: Formation and Repair Mechanisms of DNA-Protein Cross-Links, and Functions and Regulatory Mechanisms of TREX1 in DNA Repair