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We are working towards a quantitative, mechanistic, and structural description of chromatin. We are interested in the evolutionary origin of the nucleosome and study histone-based chro-matin in non-eukaryotic organisms. We also have an active research program addressing the structure, enzymology and in vivo role of poly-ADP-ribose)-polymerases, with a focus on the interactions of PARP1 and PARP2 with chromatin, its mechanism of acti-vation, and its inhibition for cancer therapies (PARP inhibitors). My lab uses a wide palette of approaches, such as x-ray crystallography, cryo-EM, analytical ultracentrifugation, affinity assays, hydrogen-deuterium exchange coupled to mass spectrometry, atomic force microscopy, and life-cell microscopy.

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• Liu, Y., K. Zhou, N. Zhang, H. Wei, Y. Z. Tan, Z. Zhang, B. Carragher, C. S. Potter, S. D'Arcy and K. Luger (2020). "FACT caught in the act of manipulating the nucleosome." Nature 577(7790): 426-431.
• Liu, Y., Bisio, H., Toner, C.M., Jeudy, S., Philippe, N., Zhou, K., Bowerman, S., White, A., Edwards, G., Abergel, C., et al. (2021). Virus-encoded histone doublets are essential and form nucleosome-like structures. Cell 184, 4237-4250 e4219.
• Rudolph, J., U. M. Muthurajan, M. Palacio, J. Mahadevan, G. Roberts, A. Erbse, P. N. Dyer and K. Luger (2021). "The BRCT Domain of PARP1 Binds Intact DNA and Mediates Intrastrand Transfer." Mol.Cell (24), 4994-5006 e4995.
• Hocher, A., Laursen, S.P., Radford, P., Tyson, J., Lambert, C., Stevens, K.M., Picardeau, M., Sockett, R.E., Luger, K. and Warnecke, T. (2023) Histone-organized chromatin in bacteria. bioRxiv, 2023.2001.2026.525422. Ìý