Originally published In Press as doi:10.1074/jbc.M305646200 on June 6, 2003
J. Biol. Chem., Vol. 278, Issue 34, 32014-32019, August 22, 2003
POLN, a Nuclear PolA Family DNA Polymerase Homologous to the DNA Cross-link Sensitivity Protein Mus308*,
Federica Marini 
,
Nayun Kim,
Anthony Schuffert and
Richard D. Wood 
From the
University of Pittsburgh Cancer Institute, Hillman Cancer Center,
Research Pavilion, Pittsburgh, Pennsylvania 15213
The Drosophila Mus308 gene is unusual in encoding both a family A
DNA polymerase domain and a DNA/RNA helicase domain. A mus308
mutation was shown to result in increased sensitivity to DNA cross-linking
agents, leading to the hypothesis that Mus308 functions in the repair of DNA
interstrand cross-links. Recently a mammalian ortholog of Mus308,
POLQ, has been identified. We report here the identification, cloning,
and characterization of POLN and its gene product, a new mammalian
DNA polymerase also related to Mus308. The human cDNA encodes a
protein of 900 amino acid residues. The region starting from residue 419
shares 33% identity (48% similarity) with the equivalent region of
Escherichia coli DNA polymerase I. POLN is expressed in
human cell lines with numerous alternatively spliced transcripts, and a
full-length human coding region that comprises 24 exons within 160 kilobases
of genomic DNA. Expression analysis by northern blotting and in situ
hybridization showed highest expression of full-length POLN in human
and mouse testis. POLN localized to the nucleus when expressed as a enhanced
green fluorescent protein (GFP)-tagged protein in human fibroblasts.
GFP-tagged recombinant POLN had DNA polymerase activity on activated calf
thymus DNA and on a singly primed template.
Received for publication, May 29, 2003
The nucleotide sequence(s) reported in this paper has been submitted to
the GenBankTM/EBI Data Bank with accession number(s) AY136549
and AY135562.
* This work was supported by the University of Pittsburgh Cancer Institute,
by Grant RO1 CA101980 from the National Institutes of Health, and by the
Imperial Cancer Research Fund (now Cancer Research UK). 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.
The on-line version of this article (available at
http://www.jbc.org)
contains supplemental "Materials and Methods," Figs. S6–S8,
and Table SI.
Current address: Universita' degli Studi di Milano, Dip. di Genetica e
Biol. dei Microorganismi, Via Celoria 26, 20133 Milano, Italy.
To whom correspondence should be addressed: University of Pittsburgh Cancer
Inst., Hillman Cancer Center, Research Pavilion, 5117 Centre Ave., Suite 2.6,
Pittsburgh, PA 15213.
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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
