Deciphering the Molecular Mechanisms of Histone H2A Variant Recognition by the ATAD2/B Bromodomains
Conference Year
2023
Abstract
ATAD2 and ATAD2B are paralogous proteins that both contain C-terminal bromodomains. These protein modules recognize and bind to acetylated lysine residues on histone N-terminal tails. In recent years, bromodomains have become attractive drug targets due to their roles in gene regulation and frequent overexpression various diseases. While the interactions between these proteins and the core histones have been studied, their ability to recognize histone variant N-terminal tails has not been previously explored. The goal of the experiments described here were to characterize the binding specificity of the ATAD2/B bromodomains for various histone H2A.X/Z N-terminal acetylation marks
Primary Faculty Mentor Name
Karen Glass
Graduate Student Mentors
Margaret Phillips
Status
Undergraduate
Student College
College of Arts and Sciences
Program/Major
Biochemistry
Primary Research Category
Life Sciences
Deciphering the Molecular Mechanisms of Histone H2A Variant Recognition by the ATAD2/B Bromodomains
ATAD2 and ATAD2B are paralogous proteins that both contain C-terminal bromodomains. These protein modules recognize and bind to acetylated lysine residues on histone N-terminal tails. In recent years, bromodomains have become attractive drug targets due to their roles in gene regulation and frequent overexpression various diseases. While the interactions between these proteins and the core histones have been studied, their ability to recognize histone variant N-terminal tails has not been previously explored. The goal of the experiments described here were to characterize the binding specificity of the ATAD2/B bromodomains for various histone H2A.X/Z N-terminal acetylation marks