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M004263200v1
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Papers In Press, published online ahead of print July 7, 2000
J. Biol. Chem, 10.1074/jbc.M004263200
Submitted on May 18, 2000
Revised on July 5, 2000
Accepted on July 6, 2000

Identification and characterization of human DNA polymerase beta2, a DNA polymerase beta-related enzyme

Kei-ichi Nagasawa, Kenzo Kitamura, Akihiro Yasui, Yuji Nimura, Kyoji Ikeda, Momoki Hirai, Akio Matsukage, and Makoto Nakanishi

Department of Biochemistry, Nagoya City University Medical School, Nagoya, Aichi 467-8601

Corresponding Author: mkt-naka{at}med.nagoya-cu.ac.jp

The BRCT (BRCA1 COOH-terminus) 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 beta2) that is closely related to DNA polymerase beta (Pol beta). The predicted Pol beta2 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 beta2 gene is expressed in a tissue-specific manner, with transcripts being most abundant in testis. A fusion construct comprising Pol beta2 and green fluorescent protein exhibited a predominantly nuclear localization in transfected HeLa cells. Recombinant human Pol beta2 from insect cells exhibited substantial DNA polymerase activity, but it did not possess terminal deoxyribonucleotidyl transferase activity. A truncated-Pol beta2 mutant lacking the BRCT motif retained substantial DNA polymerase activity, whereas a mutant Pol beta2 with two alanine point mutations within the DNA polymerase active site did not. These results indicate that Pol beta2 is a Pol beta?related DNA polymerase with a BRCT motif that is dispensable for its polymerase activity.


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