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Nucleic Acids Research Advance Access originally published online on September 4, 2009
Nucleic Acids Research 2009 37(19):6439-6453; doi:10.1093/nar/gkp720
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Nucleic Acids Research, 2009, Vol. 37, No. 19 6439-6453
© The Author(s) 2009. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/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

Biochemical properties and base excision repair complex formation of apurinic/apyrimidinic endonuclease from Pyrococcus furiosus

Shinichi Kiyonari1,2, Saki Tahara1, Tsuyoshi Shirai3,4, Shigenori Iwai5, Sonoko Ishino1,2 and Yoshizumi Ishino1,2,*

1Department of Genetic Resources Technology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, 2BIRD-Japan Science and Technology Agency, 6-10-1 Hakozaki, Fukuoka-shi, Fukuoka 812-8581, 3Department of Bioscience, Nagahama Institute of Bio-Science and Technology, 4BIRD-Japan Science and Technology Agency, 1266 Tamura, Nagahama, Shiga 526-0829 and 5Division of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan

*To whom correspondence should be addressed. Tel: +81 92 642 4217; Fax: +81 92 642 3051; Email: ishino{at}agr.kyushu-u.ac.jp

Received May 19, 2009. Revised August 14, 2009. Accepted August 15, 2009.

Apurinic/apyrimidinic (AP) sites are the most frequently found mutagenic lesions in DNA, and they arise mainly from spontaneous base loss or modified base removal by damage-specific DNA glycosylases. AP sites are cleaved by AP endonucleases, and the resultant gaps in the DNA are repaired by DNA polymerase/DNA ligase reactions. We identified the gene product that is responsible for the AP endonuclease activity in the hyperthermophilic euryarchaeon, Pyrococcus furiosus. Furthermore, we detected the physical interaction between P. furiosus AP endonuclease (PfuAPE) and proliferating cell nuclear antigen (PCNA; PfuPCNA) by a pull-down assay and a surface plasmon resonance analysis. Interestingly, the associated 3'–5' exonuclease activity, but not the AP endonuclease activity, of PfuAPE was stimulated by PfuPCNA. Immunoprecipitation experiments using the P. furiosus cell extracts supported the interaction between PfuAPE and PfuPCNA in the cells. This is the first report describing the physical and functional interactions between an archaeal AP endonuclease and PCNA. We also detected the ternary complex of PfuPCNA, PfuAPE and Pfu uracil-DNA glycosylase. This complex probably functions to enhance the repair of uracil-containing DNA in P. furiosus cells.


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