Date of Completion


Thesis Type

College of Arts and Science Honors


Department of Pharmacology

First Advisor

Karen Glass


biochemistry, epigenetics, cancer


Cancer is the second leading cause of death worldwide, and many different processes in our bodies can play a role in the progression of this disease. In order to find specific and effective treatments for cancer and improve survival rate, we must understand how these processes work at the molecular level. The ATPase family AAA+ domain-containing protein 2 (ATAD2) is a well-studied epigenetic reader that is up-regulated in several forms of cancer, such as breast, lung, gastric, endometrial, renal, and prostate, however, its underlying mechanism and overall function remains unclear. ATAD2 contains two AAA+ ATPase domains, a bromodomain, and a C-terminal domain that function to recognize acetylated lysine on the N-terminal tails of histone H4, and it’s been speculated that ATAD2 oligomerizes upon recognition. In this study we aimed to characterize the histone binding partners of the ATAD2 bromodomain and to understand the functional role of the C-terminal domain in ATAD2B, a conserved paralog of ATAD2. Using protein purification methods, isothermal titration calorimetry, and size-exclusion chromatography, we found that multiple acetylation and methylation modifications impact the ability of the ATAD2 bromodomain to bind to acetylated histone ligands, and that the C-terminal domain of ATAD2B is not necessary for protein oligomerization. These results provide a better understanding of the role of ATAD2/B in processes that lead to cancer and how it can be used as a drug target.

Available for download on Friday, May 08, 2026