Methods and applications of site-specific acetylation of histones
Graduate Student Christie Cade
By Christie Cade
In the nature vs. nurture debate, some people argue that we are who we are based on our genetic code and thus “nature.” Other people argue that we are a product of our environment, or “nurture.” The field of epigenetics brings a whole new idea to the table: our ancestors’ environments or our environment can affect which genes are made into protein at a given time, thus drawing on both nature and nurture. One way the environment can affect the genes is by modifying the proteins called histones that DNA is wrapped around. These modifications cause the DNA to become more or less tightly wrapped, and thus more or less accessible to the cellular machinery used for making proteins.
HAT=histone acetyl transferase
One modification which generally makes the DNA more accessible is acetylation of an amino acid called lysine at various positions on the histone. Many techniques exist for studying the cellular effects of acetylation at each position. However, it is difficult to understand at a molecular level how this works. Several techniques have recently emerged to allow researchers to study homogeneous populations of modified histones: enzymatic modification of histones, native chemical ligation, and unnatural amino acid mutagenesis.