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Originally published In Press as doi:10.1074/jbc.M106990200 on October 10, 2001

J. Biol. Chem., Vol. 276, Issue 52, 49258-49266, December 28, 2001
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Mediation of Proliferating Cell Nuclear Antigen (PCNA)-dependent DNA Replication through a Conserved p21Cip1-like PCNA-binding Motif Present in the Third Subunit of Human DNA Polymerase delta *

Manuelle DucouxDagger §, Serge UrbachDagger , Giuseppe BaldacciDagger , Ulrich Hübscher, Stéphane Koundrioukoff, Jesper Christensen||, and Patrick HughesDagger **

From the Dagger  Institut Curie, UMR 2027 du CNRS, Génotoxicologie et Cycle Cellulaire, Bâtiment 110, Centre Universitaire, 91405 Orsay Cedex, France,  Department of Veterinary Biochemistry, University Zürich-Irchel, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland, and the || Department of Microbiology and Immunology, University of Copenhagen, Blegdamsvej 3b, Building 24.2, Kopenhaven 2200, Denmark

The subunit that mediates binding of proliferating cell nuclear antigen (PCNA) to human DNA polymerase delta  has not been clearly defined. We show that the third subunit of human DNA polymerase delta , p66, interacts with PCNA through a canonical PCNA-binding sequence located in its C terminus. Conversely, p66 interacts with the domain-interconnecting loop of PCNA, a region previously shown to be important for DNA polymerase delta  activity and for binding of the cell cycle inhibitor p21Cip1. In accordance with this, a peptide containing the PCNA-binding domain of p21Cip1 inhibited p66 binding to PCNA and the activity of native three-subunit DNA polymerase delta . Furthermore, pull-down assays showed that DNA polymerase delta  requires p66 for interaction with PCNA. More importantly, only reconstituted three-subunit DNA polymerase delta  displayed PCNA-dependent DNA replication that could be inhibited by the PCNA-binding domain of p21Cip1. Direct participation of p66 in PCNA-dependent DNA replication in vivo is demonstrated by co-localization of p66 with PCNA and DNA polymerase delta  within DNA replication foci. Finally, in vitro phosphorylation of p66 by cyclin-dependent kinases suggests that p66 activity may be subject to cell cycle-dependent regulation. These results suggest that p66 is the chief mediator of PCNA-dependent DNA synthesis by DNA polymerase delta .

* This work was supported in part by Training and Mobility of Researchers Contract ERB FMRX-CT97-0125 from the European Union, by Grant 9945 (to G. B.) from the Association pour la Recherche contre le Cancer, and by the Swiss National Science Foundation Grant 31-61361.00 (to U. H.).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.

§ Recipient of a stipend from the Ligue National Contre le Cancer during the course of this study.

** To whom correspondence may be addressed. Tel.: 33-1-69863062; Fax: 33-1-69869429; E-mail: hughes@curie.u-psud.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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