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M510314200v1
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Papers In Press, published online ahead of print February 28, 2006
J. Biol. Chem, 10.1074/jbc.M510314200
Submitted on September 20, 2005
Revised on February 27, 2006
Accepted on February 28, 2006

Postreplicative mismatch repair factors are recruited to epstein-barr virus replication compartments

Tohru Daikoku, Ayumi Kudoh, Yutaka Sugaya, Satoko Iwahori, Noriko Shirata, Hiroki Isomura, and Tatsuya Tsurumi

Division of Virology, Aichi Cancer Center Research Institute, Nagoya, Aichi 464-8681

Corresponding Author: ttsurumi{at}aichi-cc.jp

The mismatch repair (MMR) system, highly conserved throughout evolution, corrects nucleotide mispairing that arises during cellular DNA replication. We report here that proliferating cell nuclear antigen (PCNA), the clamp loader complex (RF-C), and a series of MMR proteins like MSH-2, MSH-6, MLH1 and hPSM2 can be assembled to Epstein-Barr virus replication compartments, the sites of viral DNA synthesis. Levels of the DNA-bound form of PCNA increased with progression of viral productive replication. BrdUrd-labeled chromatin immunodepletion analyses confirmed that PCNA is loaded onto newly synthesized viral DNA as well as BALF2 and BMRF1 viral proteins during lytic replication. Furthermore, the anti-PCNA, -MSH2, -MSH3, or -MSH6 antibody could immunoprecipitate BMRF1 replication protein probably via viral DNA genome. PCNA loading might trigger transfer of a series of host MMR proteins to the sites of viral DNA synthesis. The MMR factors might function for the repair of mismatches that arise during viral replication or act to inhibit recombination between moderately divergent (homeologous) sequences.


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