If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.


Biological Chemistry

Histone Acetylation Allows DNA Unpacking

ACS Meeting News: Modeling study hints at how the modification activates gene expression

by Jyllian Kemsley
April 2, 2012 | A version of this story appeared in Volume 90, Issue 14

Acetylation of the tail of histone protein H4 is a key modification known to play a role in activating gene expression. Structural modeling studies by Garegin A. Papoian and Davit Potoyan of the University of Maryland now illuminate how the modification may work. To pack into chromosomes, DNA wraps around histone octamers, and the DNA-histone complexes further coil into fibers. Although histone tails are intrinsically disordered, Papoian and Potoyan still find that the proteins have conformational preferences. Unacetylated, the H4 tail of a DNA-histone complex can stretch out to interact with adjacent complexes, perhaps facilitating fiber formation, Papoian suggested. Acetylation of the tail at a lysine residue, however, induces a more compact structure that causes the tail to interact more strongly with its own DNA. The acetylated tail would then be unavailable for complex-complex interactions and would enable gene expression by allowing DNA-histone fibers to unwind.

C&EN Covers The ACS National Meeting

Want the scoop on the ACS meeting in San Diego? Check out C&EN Picks, a series of videos that spotlight sessions selected by C&EN staff. Reporters also fan out across the meeting to bring you news coverage. Find it all collected at C&EN's meeting page,


This article has been sent to the following recipient:

Chemistry matters. Join us to get the news you need.