HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 16, 11422-11430, April 21, 2006

This Article Full Text Full Text (PDF) All Versions of this Article: 281/16/11422    most recent M510314200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Daikoku, T. Articles by Tsurumi, T. Search for Related Content PubMed PubMed Citation Articles by Daikoku, T. Articles by Tsurumi, T. Social Bookmarking                      What's this?

Postreplicative Mismatch Repair Factors Are Recruited to Epstein-Barr Virus Replication Compartments^*

From the Division of Virology, Aichi Cancer Center Research Institute, 1-1 Kanokoden, Chikusa-ku, Nagoya 464-8681, Japan

The mismatch repair (MMR) system, highly conserved throughout evolution, corrects nucleotide mispairing that arise 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. Bromodeoxyuridine-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 antibodies could immunoprecipitate BMRF1 replication protein probably via the 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 (homologous) sequences.

Received for publication, September 20, 2005 , and in revised form, February 27, 2006.

^* This work was supported by grants-in-aid for Scientific Research on Priority Areas from the Ministry of Education, Science, Sports, Culture and Technology of Japan (15390153, 17659138, and 16017322) (to T. T.) and the Uehara Memorial Foundation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 81-52-764-2979; Fax: 81-52-764-2979; E-mail: ttsurumi{at}aichi-cc.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C.-C. Lu, Y.-C. Chen, J.-T. Wang, P.-W. Yang, and M.-R. Chen Xeroderma pigmentosum C is involved in Epstein Barr virus DNA replication J. Gen. Virol., December 1, 2007; 88(12): 3234 - 3243. [Abstract] [Full Text] [PDF]

				C.-C. Lu, H.-T. Huang, J.-T. Wang, G. Slupphaug, T.-K. Li, M.-C. Wu, Y.-C. Chen, C.-P. Lee, and M.-R. Chen Characterization of the Uracil-DNA Glycosylase Activity of Epstein-Barr Virus BKRF3 and Its Role in Lytic Viral DNA Replication J. Virol., February 1, 2007; 81(3): 1195 - 1208. [Abstract] [Full Text] [PDF]