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Originally published In Press as doi:10.1074/jbc.M200065200 on May 1, 2002

J. Biol. Chem., Vol. 277, Issue 27, 24340-24345, July 5, 2002
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Direct Interaction of Proliferating Cell Nuclear Antigen with the Small Subunit of DNA Polymerase delta *

Xiaoqing LuDagger , Cheng-Keat TanDagger , Jin-Qiu ZhouDagger §, Min You, L. Michael Carastro||, Kathleen M. DowneyDagger , and Antero G. SoDagger **

From the Departments of Dagger  Medicine and  Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33101

The interaction between proliferating cell nuclear antigen (PCNA) and DNA polymerase delta  is essential for processive DNA synthesis during DNA replication/repair; however, the identity of the subunit of DNA polymerase delta  that directly interacts with PCNA has not been resolved until now. In the present study we have used reciprocal co-immunoprecipitation experiments to determine which of the two subunits of core DNA polymerase delta , the 125-kDa catalytic subunit or the 50-kDa small subunit, directly interacts with PCNA. We found that PCNA co-immunoprecipitated with human p50, as well as calf thymus DNA polymerase delta  heterodimer, but not with p125 alone, suggesting that PCNA directly interacts with p50 but not with p125. A PCNA-binding motif, similar to the sliding clamp-binding motif of bacteriophage RB69 DNA polymerase, was identified in the N terminus of p50. A 22-amino acid oligopeptide containing this sequence (MRPFL) was shown to bind PCNA by far Western analysis and to compete with p50 for binding to PCNA in co-immunoprecipitation experiments. The binding of p50 to PCNA was inhibited by p21, suggesting that the two proteins compete for the same binding site on PCNA. These results establish that the interaction of PCNA with DNA polymerase delta  is mediated through the small subunit of the enzyme.

* This work was supported by Grant DK26206 from the National Institutes of Health and in part by funds from the Sylvester Comprehensive Cancer Center.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China.

|| Present address: Salk Inst. for Biological Studies, Gene Expression Laboratories, La Jolla, CA 92037.

** To whom correspondence should be addressed: Dept. of Medicine (R99), University of Miami School of Medicine, P.O. Box 016960, Miami, FL 33101. Tel.: 305-243-6304; Fax: 305-243-4519; E-mail: aso@med.miami.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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