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Originally published In Press as doi:10.1074/jbc.M004263200 on July 7, 2000

J. Biol. Chem., Vol. 275, Issue 40, 31233-31238, October 6, 2000
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Identification and Characterization of Human DNA Polymerase beta 2, a DNA Polymerase beta -Related Enzyme*

Kei-ichi NagasawaDagger §, Kenzo Kitamura||, Akihiro Yasui§, Yuji Nimura, Kyoji IkedaDagger , Momoki Hirai**, Akio MatsukageDagger Dagger §§, and Makoto NakanishiDagger ||¶¶

From the Dagger  Department of Geriatric Research, National Institute for Longevity Sciences, Obu, Aichi 474-8522, § Department of Surgery, National Chubu Hospital, Obu, Aichi 474-8511,  Department of Surgery, Nagoya University Medical School, Nagoya, Aichi 466-8550, || Department of Biochemistry, Nagoya City University Medical School, Nagoya, Aichi 467-8601, ** Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113, and Dagger Dagger  Laboratory of Cell Biology, Aichi Cancer Center Research Institute, Nagoya, Aichi 464-8681, Japan

The BRCA1 COOH terminus (BRCT) motif is present in many nuclear proteins that contribute to cell cycle regulation or DNA repair. Polymerase chain reaction-based screening with degenerate primers targeted to the BRCT motif resulted in the isolation of a human cDNA for a previously unidentified DNA polymerase (designated DNA polymerase beta 2) that is closely related to DNA polymerase beta  (Pol beta ). The predicted Pol beta 2 protein contains a BRCT motif in its NH2-terminal region; its COOH-terminal region exhibits 33% sequence identity to a corresponding region of human Pol beta . The Pol beta 2 gene is expressed in a tissue-specific manner, with transcripts being most abundant in testis. A fusion construct comprising Pol beta 2 and green fluorescent protein exhibited a predominantly nuclear localization in transfected HeLa cells. Recombinant human Pol beta 2 from insect cells exhibited substantial DNA polymerase activity, but it did not possess terminal deoxyribonucleotidyl transferase activity. A truncated Pol beta 2 mutant lacking the BRCT motif retained substantial DNA polymerase activity, whereas a mutant Pol beta 2 with two alanine point mutations within the DNA polymerase active site did not. These results indicate that Pol beta 2 is a Pol beta -related DNA polymerase with a BRCT motif that is dispensable for its polymerase activity.

* This work was supported in part by a grant-in-aid for scientific research on priority areas from the Ministry of Education, Science, Sports, and Culture of Japan (to M. N.), by a grant-in-aid for scientific research from the Japan Society for the Promotion of Science (to M. N.), and by a health science research grant for research on the human genome and gene therapy from the Ministry of Health and Welfare of Japan (H10-genome-001 to K. I.).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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF283478.

§§ Present address: Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyou-ku, Tokyo 112-8681, Japan.

¶¶ To whom correspondence should be addressed: Dept. of Biochemistry, Nagoya City University Medical School, 1 Kawasumi, Mizuho-cho, Mizuho-ku, Nagoya 467-8601, Japan. Tel.: 81-52-853-8145; Fax: 81-52-842-3955; E-mail: mkt-naka@med.nagoya-cu.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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