Abstract
AP-endonuclease (APE) plays a central role in the base excision repair process for oxidative and alkylation damage in DNA. The major human APE with 318 amino acid residues possesses transcriptional regulatory activities for which the N-terminal region was found to be essential. Systematic deletion studies of both amino and carboxyl termini of the human APE have shown that the carboxyl termini residues are essential for the endonuclease activity as indicated by direct measurement of enzyme activity and from studies on phenotypic rescue of Escherichia coli. However, the amino-terminal residues are dispensable for this activity and the boundary of the active endonuclease lies at this end between positions 61 and 80.