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M207297200v1
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Papers In Press, published online ahead of print September 12, 2002
J. Biol. Chem, 10.1074/jbc.M207297200
Submitted on July 19, 2002
Revised on September 9, 2002
Accepted on September 12, 2002

Lesion bypass activities of human DNA polymerase mu

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

Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40536

Corresponding Author: zwang{at}uky.edu

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


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