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Title
Japanese: 
English:Mutagenic and Nonmutagenic Bypass of DNA Lesions by Drosophila DNA Polymerases dpolη and dpolι 
Author
Japanese: Ishikawa, T., Uematsu, N., Mizukoshi, T., Iwai, S., 岩崎博史, Masutani, C., Hanaoka, F., Ueda, R., Ohmori, H., Todo, T..  
English: Ishikawa, T., Uematsu, N., Mizukoshi, T., Iwai, S., Hiroshi Iwasaki, Masutani, C., Hanaoka, F., Ueda, R., Ohmori, H., Todo, T..  
Language English 
Journal/Book name
Japanese:Journal of Biological Chemistry 
English:Journal of Biological Chemistry 
Volume, Number, Page Vol. 276    No. 18    pp. 15155-15163
Published date May 2001 
Publisher
Japanese: 
English: 
Conference name
Japanese: 
English: 
Conference site
Japanese: 
English: 
Official URL http://www.scopus.com/inward/record.url?eid=2-s2.0-0035805532&partnerID=MN8TOARS
 
DOI https://doi.org/10.1074/jbc.M009822200
Abstract 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 dpoletaDeltaC and dpoliotaDeltaC, respectively, exhibit DNA polymerase activity. dpoletaDeltaC and dpoliotaDeltaC efficiently bypass a cis-syn-cyclobutane thymine-thymine (TT) dimer in a mostly error-free manner. dpoletaDeltaC 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. dpoliotaDeltaC 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'(2)C 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 dpoletaDeltaC 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.

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