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.
Authors
- Cameron Bryan (ORCID: https://orcid.org/0000-0002-2303-8189)
- Kun Yang (ORCID: https://orcid.org/0000-0001-5532-8810)
Institutions
- Austin College (US)
- The University of Texas at Austin (US)
Publication Details
- Journal
- ChemBioChem
- Published
- 2024-10-10
- DOI
- https://doi.org/10.1002/cbic.202400705
- Citations
- 1
- Primary Topic
- DNA Repair Mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.23
Funders
- Harvey Mudd College
- University of Texas at Austin
- National Institutes of Health
- National Institute of General Medical Sciences