Les Miserables and the histone code


Dr. Greg Buhrman

Dr. Greg Buhrman - First Time Teacher

By Greg Buhrman

OK, I admit I was getting a little desperate today. I’d started this class with the idea of teaching Cell Biology and along the way, explaining how normal cellular biology relates to the disease state, with a focus on cancer and diabetes. When I started organizing the class it made sense at the time. After all, I’ve spent the last ten years doing cancer research, mostly with Dr. Carla Mattos (my thesis mentor) and Dr. Jason Haugh (a committee member and collaborator in the Chemical Engineering Department) at NCSU and for a year or two (one year in his lab, two years if you count collaboration time) with Dr. Johannes Rudolph at Duke Univ. With that experience, I felt like I had a reasonable handle on enough aspects of cancer research to teach it. Diabetes is a disease that I’m just starting to work on now in Dr. Bob Rose’s lab at NCSU, so I felt like if I’m going to be learning about it anyway, I might as well incorporate it in the class.

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How hats, baby toys, and amber help us learn more about the nature vs. nurture debate

 

Methods and applications of site-specific acetylation of histones 

christie cade

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.
histone acetyl transferase

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.

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