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Published online 23 April 2004

Nucleic Acids Research, 2004, Vol. 32, No. 7 2193-2201
© 2004 Oxford University Press

XRCC1 co-localizes and physically interacts with PCNA

Jinshui Fan, Marit Otterlei1, Heng-Kuan Wong, Alan E. Tomkinson2 and David M. Wilson, III*

Laboratory of Molecular Gerontology, National Institute on Aging, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA, 1 Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, N-7489, Trondheim, Norway and 2 Radiation Oncology Research Laboratory, Department of Radiation Oncology and Greenbaum Cancer Center, University of Maryland Medical Center, 655 West Baltimore Street, Baltimore, MD 21201, USA

*To whom correspondence should be addressed. Tel: +1 410 558 8153; Fax: +1 410 558 8157; Email: wilsonda{at}grc.nia.nih.gov
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

Received March 8, 2004; Revised and Accepted March 30, 2004

X-ray Repair Cross Complementing 1 (XRCC1) is thought to function as a scaffolding protein in both base excision repair and single-strand break repair (SSBR), since it interacts with several proteins participating in these related pathways and has no known enzymatic activity. Moreover, studies indicate that XRCC1 possesses discrete G1 and S phase-specific functions. To further define the contribution of XRCC1 to DNA metabolism, we determined the in vivo localization pattern of this protein and searched for novel protein interactors. We report here that XRCC1 co-localizes with proliferating cell nuclear antigen (PCNA) at DNA replication foci, observed exclusively in the S phase of undamaged HeLa cells. Furthermore, fluorescence resonance energy transfer (FRET) analysis and co-immunoprecipitation indicate that XRCC1 and PCNA are in a complex and likely physically interact in vivo. In vitro biochemical analysis demonstrated that these two proteins associate directly, with the interaction being mediated by residues between amino acids 166 and 310 of XRCC1. The current evidence suggests a model where XRCC1 is sequestered via its interaction with PCNA to sites of DNA replication factories to facilitate efficient SSBR in S phase.


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