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Structure and function relationships in mammalian DNA polymerases

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Abstract

DNA polymerases are vital for the synthesis of new DNA strands. Since the discovery of DNA polymerase I in Escherichia coli, a diverse library of mammalian DNA polymerases involved in DNA replication, DNA repair, antibody generation, and cell checkpoint signaling has emerged. While the unique functions of these DNA polymerases are differentiated by their association with accessory factors and/or the presence of distinctive catalytic domains, atomic resolution structures of DNA polymerases in complex with their DNA substrates have revealed mechanistic subtleties that contribute to their specialization. In this review, the structure and function of all 15 mammalian DNA polymerases from families B, Y, X, and A will be reviewed and discussed with special emphasis on the insights gleaned from recently published atomic resolution structures.

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Acknowledgements

Nicole M. Hoitsma and Dr. Amy M. Whitaker are co-authors and equally contributed to this paper. This work was supported by the National Institutes of Environmental Health Sciences of the National Institutes of Health under award number R35GM128562. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

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  1. Nicole M. Hoitsma and Amy M. Whitaker contributed equally.

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  1. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA

    Nicole M. Hoitsma, Amy M. Whitaker, Matthew A. Schaich, Mallory R. Smith, Max S. Fairlamb & Bret D. Freudenthal

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Hoitsma, N.M., Whitaker, A.M., Schaich, M.A. et al. Structure and function relationships in mammalian DNA polymerases. Cell. Mol. Life Sci. 77, 35–59 (2020). https://doi.org/10.1007/s00018-019-03368-y

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