Thomas Hollis, PhD, Wake Forest School of Medicine

Thomas Hollis, PhD
Thomas Hollis, PhD

Research in the Hollis laboratory focuses on the structural biology of proteins involved in DNA repair. The lab uses a combination of X-ray crystallography, biochemistry and molecular biology to address questions of DNA damage recognition and repair by proteins.

Read Dr. Hollis's related blog post, A New Avenue for Protein-Nucleic Acid Complex Crystallization »

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References

  1. Pryor EE Jr, Wozniak DJ, Hollis, T. Crystallization of Pseudomonas aeruginosa AmrZ protein: development of a comprehensive method for obtaining and optimization of protein-DNA crystals. Acta Crystallographica Section F. 2012; F68: 985-993.
  2. Pryor EE Jr, Waligora EA, Xu B, Dellos-Nolan S, Wozniak DJ, et al. The Transcription Factor AmrZ Utilizes Multiple DNA Binding Modes to Recognize Activator and Repressor Sequences of Pseudomonas aeruginosa Virulence Genes. PLoS Pathogens. 2012; 8(4): e1002648.
  3. Holland PJ, Hollis T. Structural and mutational analysis of Escherichia coli AlkB provides insight into substrate specificity and DNA damage searching. PLoS ONE. 2010; 5(1): e8680.
  4. de Silva U, Perrino FW, Hollis T. DNA binding induces active site conformational change in the human TREX2 3'-exonuclease. Nucleic Acids Res. 2009; 37(7):2411-2417.
  5. de Silva U, Choudhury S, Bailey SL, Harvey S, Perrino FW, Hollis T. The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering. J Biol Chem. 2007; 282(14):10537-43
  6. Hollis T. Crystallization of protein-DNA complexes. In Methods Mol Biol. (ed. Doublie) 2007; 363():225-237.