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J. Biol. Chem., Vol. 280, Issue 23, 22375-22384, June 10, 2005

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Further Characterization of Human DNA Polymerase Interacting Protein 38^*

Bin Xie, Hao Li, Qi Wang¶, Suqing Xie¶, Amal Rahmeh, Wei Dai¶, and Marietta Y. W. T. Lee||

From the Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla, New York 10595 and the ^¶Department of Medicine, New York Medical College, Valhalla, New York 10595

Polymerase interacting protein 38 (PDIP38) was identified as a human DNA polymerase (pol) interacting protein through a direct interaction with p50, the small subunit of human pol . PDIP38 was also found to interact with proliferating cell nuclear antigen, which suggested that it might play a role in vivo in the processes of DNA replication and DNA repair in the nucleus. In order to characterize further this novel protein, we have examined its subcellular localization by the use of immunochemical and cellular fractionation techniques. These studies show that PDIP38 is a novel mitochondrial protein and is localized mainly to the mitochondria. PDIP38 was shown to possess a functional mitochondrial targeting sequence that is located within the first 35 N-terminal amino acid residues. The mature PDIP38 protein is about 50 amino acid residues smaller than the full-length precursor PDIP38 protein, consistent with it being processed by cleavage of the mitochondrial targeting sequence during entry into the mitochondria. His-tagged mature PDIP38 inhibited pol activity in vitro and interacted with human papillomavirus 16 E7 oncoprotein, suggesting that PDIP38 might play a role in the pol -mediated viral DNA replication. Although the localization of PDIP38 to the mitochondria suggests that it serves functions within the mitochondria, we cannot eliminate the possibility that it may be involved in pol -mediated DNA replication or DNA repair under certain conditions such as viral infection.

Received for publication, December 27, 2004 , and in revised form, March 31, 2005.

^* This work was supported by National Institutes of Health Grant GM31973, by Philip Morris U. S., Inc., and Philip Morris International (to M. Y. W. T. L.), and by National Institutes of Health Grant CA 74299 (to W. D.). 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.

Both authors contributed equally to this work.

^|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, New York Medical College, Valhalla, NY 10595. Tel.: 914-594-4070; Fax: 914-594-4058; E-mail: Marietta_Lee{at}nymc.edu.

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