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J. Biol. Chem., Vol. 277, Issue 46, 44582-44587, November 15, 2002

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Lesion Bypass Activities of Human DNA Polymerase µ^*

Yanbin Zhang, Xiaohua Wu, Dongyu Guo, Olga Rechkoblit^§, John-Stephen Taylor^¶, Nicholas E. Geacintov^§, and Zhigang Wang

From the  Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 40536, ^§ Chemistry Department, New York University, New York, New York 10003, and ^¶ Department of Chemistry, Washington University, St. Louis, Missouri 63130

DNA polymerase µ (Polµ) is a newly discovered member of the polymerase X family with unknown cellular function. The understanding of Polµ function should be facilitated by an understanding of its biochemical activities. By using purified human Polµ for biochemical analyses, we discovered the lesion bypass activities of this polymerase in response to several types of DNA damage. When it encountered a template 8-oxoguanine, abasic site, or 1,N⁶-ethenoadenine, purified human Polµ efficiently bypassed the lesion. Even bulky DNA adducts such as N-2-acetylaminofluorene-adducted guanine, (+)- and ()-trans-anti-benzo[a]pyrene-N²-dG were unable to block the polymerase activity of human Polµ. Bypass of these simple base damage and bulky adducts was predominantly achieved by human Polµ through a deletion mechanism. The Polµ specificity of nucleotide incorporation indicates that the deletion resulted from primer realignment before translesion synthesis. Purified human Polµ also effectively bypassed a template cis-syn TT dimer. However, this bypass was achieved in a mainly error-free manner with AA incorporation opposite the TT dimer. These results provide new insights into the biochemistry of human Polµ and show that efficient translesion synthesis activity is not strictly confined to the Y family polymerases.

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