Journal article

Publication year: 2000

Pages: 28433-28438

Journal: Journal of Biological Chemistry

Volume number: 275

Issue number: 37

ISSN: 0021-9258

DOI Link: https://doi.org/10.1074/jbc.M001064200

Publisher: Elsevier

Abstract: 
Human 3-methyladenine-DNA glycosylase (MPG protein) initiates base excision repair by severing the glycosylic bond of numerous damaged bases. In comparison, homologues of the Rad23 proteins (hHR23) and the hXPC protein are involved in the recognition of damaged bases in global genome repair, a subset of nucleotide excision repair. In this report, we show that the hHR23A and -B also interact with the MPG protein and can serve as accessory proteins for DNA damage recognition in base excision repair. Furthermore, the MPG.hHR23 protein complex elevates the rate of MPG protein-catalyzed excision from hypoxanthine-containing substrates. This increased excision rate is correlated with a greater binding affinity of the MPG protein-hHR23 protein complex for damaged DNA. These data suggest that the hHR23 proteins function as universal DNA damage recognition accessory proteins in both of these major excision repair pathways.

Harvard Citation style: Miao, F., Bouziane, M., Dammann, R., Masutani, C., Hanaoka, F., Pfeifer, G., et al. (2000) 3-methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteins, Journal of Biological Chemistry, 275(37), pp. 28433-28438. https://doi.org/10.1074/jbc.M001064200

APA Citation style: Miao, F., Bouziane, M., Dammann, R., Masutani, C., Hanaoka, F., Pfeifer, G., & O'Connor, T. (2000). 3-methyladenine-DNA glycosylase (MPG protein) interacts with human RAD23 proteins. Journal of Biological Chemistry. 275(37), 28433-28438. https://doi.org/10.1074/jbc.M001064200