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Originally published In Press as doi:10.1074/jbc.M009822200 on January 31, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15155-15163, May 4, 2001
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Mutagenic and Nonmutagenic Bypass of DNA Lesions by Drosophila DNA Polymerases dpoleta and dpoliota *

Tomoko IshikawaDagger , Norio UematsuDagger , Toshimi Mizukoshi§, Shigenori Iwai§, Hiroshi Iwasaki, Chikahide Masutani||, Fumio Hanaoka||, Ryu Ueda**, Haruo OhmoriDagger Dagger , and Takeshi TodoDagger §§

From the Dagger  Radiation Biology Center, Kyoto University, Kyoto 606-8501, § Biomolecular Engineering Research Institute, Suita, Osaka 565-0874,  Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, || Institute for Molecular and Cellular Biology, Osaka University, Suita, Osaka 565-0871, ** Mitsubishi Kasei Institute of Life Sciences, Machida, Tokyo 194-8511, and Dagger Dagger  Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan

cDNA sequences were identified and isolated that encode Drosophila homologues of human Rad30A and Rad30B called drad30A and drad30B. Here we show that the C-terminal-truncated forms of the drad30A and drad30B gene products, designated dpoleta Delta C and dpoliota Delta C, respectively, exhibit DNA polymerase activity. dpoleta Delta C and dpoliota Delta C efficiently bypass a cis-syn-cyclobutane thymine-thymine (TT) dimer in a mostly error-free manner. dpoleta Delta C shows limited ability to bypass a 6-4-photoproduct ((6-4)PP) at thymine-thymine (TT-(6-4)PP) or at thymine-cytosine (TC-(6-4)PP) in an error-prone manner. dpoliota Delta C scarcely bypasses these lesions. Thus, the fidelity of translesion synthesis depends on the identity of the lesion and on the polymerase. The human XPV gene product, hpoleta , bypasses cis-syn-cyclobutane thymine-thymine dimer efficiently in a mostly error-free manner but does not bypass TT-(6-4)PP, whereas Escherichia coli DNA polymerase V (UmuD'2C complex) bypasses both lesions, especially TT-(6-4)PP, in an error-prone manner (Tang, M., Pham, P., Shen, X., Taylor, J. S., O'Donnell, M., Woodgate, R., and Goodman, M. F. (2000) Nature 404, 1014-1018). Both dpoleta Delta C and DNA polymerase V preferentially incorporate GA opposite TT-(6-4)PP. The chemical structure of the lesions and the similarity in the nucleotides incorporated suggest that structural information in the altered bases contribute to nucleotide selection during incorporation opposite these lesions by these polymerases.

* This work was supported by Grants-in-aid from the ministry of Education, Science, Sports, and Culture of Japan 09308020, 11146206, 11480140, 11878093 and by the REIMEI Research Resources of Japan Atomic Energy Research Institute.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) AB049435 (DmRev1), AB049433 (DmRAD30A), and AB049434 (DmRAD30B).

§§ To whom correspondence should be addressed: Radiation Biology Center, Kyoto University, Yoshidakonoe-cho, Sakyoku, Kyoto 606-8501, Japan. Tel.: 81-75-753-7555; Fax: 81-75-753-7564; E-mail: todo@house.rbc.kyoto-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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