Scientific background: |
APEX2, also called apurinic/apyrimidinic endonuclease like-2, is a member of the apurinic/apyrimidinic (AP) family of endonucleases that initiate the repair of AP sites formed by spontaneous hydrolysis of the N-glycosylic bond, mutagen-induced base release, or damaged-base excision by a DNA repair glycosylase. RT-PCR detected APEX2 expression in HeLa cells, Jurkat cells, and human kidney, brain and fetal brain tissue.The APEX2 gene contains 6 exons. The APEX2 gene is mapped to chromosome Xp11.21. APEX2 participates in both nuclear and mitochondrial base excision repair (BER). APEX2 displayed weaker AP site-specific and 3-prime nuclease activities compared to APEX1. APEX2 plays a role in processing 3-prime-damaged termini or 3-prime-mismatched nucleotides. |
References: |
1. Burkovics, P., Szukacsov, V., Unk, I., Haracska, L.Human Ape2 protein has 3-5-prime exonuclease activity that acts preferentially on mismatched base pairs.Nucleic Acids Res. 34: 2508-2515, 2006.
2. Hadi, M. Z., Ginalski, K., Nguyen, L. H., Wilson, D. M., III.Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III.J. Molec. Biol. 316: 853-866, 2002.
3. Tsuchimoto, D., Sakai, Y., Sakumi, K., Nishioka, K., Sasaki, M., Fujiwara, T., Nakabeppu, Y.Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen.Nucleic Acids Res. 29: 2349-2360, 2001
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