Human APE2 and TREX2 Repair 3'-DNA-Peptide Cross-links Derived from Abasic Sites.
Xiaoying Wei, Joel Cepeda, Jee Min Chung, Sang Eun Lee, Kun Yang
Abstract
Open AccessHistones react with one of the most abundant endogenous DNA lesions, the apurinic/apyrimidinic (abasic, AP) site, to form reversible but long-lived Schiff base DNA-protein cross-links at 3'-DNA termini (3'-histone-DPCs). These DPCs need to be repaired, because 3'-hydroxyl groups are required for DNA repair synthesis and strand ligation. We previously identified three human enzymes, including tyrosyl-DNA phosphodiesterase 1, AP endonuclease 1 (APE1), and three-prime repair exonuclease 1 (TREX1), that can repair chemically synthesized adducts that closely resemble the proteolyzed Schiff base 3'-histone-DPCs. Here, we report another two human enzymes, APE2 and TREX2, that have a similar function.