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Nucleic Acids Research Advance Access published online on May 13, 2009
Nucleic Acids Research, doi:10.1093/nar/gkp357
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© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Genome Integrity, Repair and Replication

Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'–5' exonuclease activities of human Ape2 in repair of oxidative DNA damage

Peter Burkovics, Ildikó Hajdú, Valéria Szukacsov, Ildiko Unk and Lajos Haracska*

Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Temesvari krt. 62, Szeged, H-6701, Hungary

*To whom correspondence should be addressed. Tel/Fax: +36 62 599666; Email: haracska{at}brc.hu

Received February 17, 2009. Revised April 21, 2009. Accepted April 22, 2009.

Human Ape2 protein has 3' phosphodiesterase activity for processing 3'-damaged DNA termini, 3'–5' exonuclease activity that supports removal of mismatched nucleotides from the 3'-end of DNA, and a somewhat weak AP-endonuclease activity. However, very little is known about the role of Ape2 in DNA repair processes. Here, we examine the effect of interaction of Ape2 with proliferating cell nuclear antigen (PCNA) on its enzymatic activities and on targeting Ape2 to oxidative DNA lesions. We show that PCNA strongly stimulates the 3'–5' exonuclease and 3' phosphodiesterase activities of Ape2, but has no effect on its AP-endonuclease activity. Moreover, we find that upon hydrogen-peroxide treatment Ape2 redistributes to nuclear foci where it colocalizes with PCNA. In concert with these results, we provide biochemical evidence that Ape2 can reduce the mutagenic consequences of attack by reactive oxygen species not only by repairing 3'-damaged termini but also by removing 3'-end adenine opposite from 8-oxoG. Based on these findings we suggest the involvement of Ape2 in repair of oxidative DNA damage and PCNA-dependent repair synthesis.


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