Probing allostery through DNA

Sangjin Kim, Erik Broströmer, Dong Xing, Jianshi Jin, Shasha Chong, Hao Ge, Siyuan Wang, Chan Gu, Lijiang Yang, Yi Qin Gao, Xiao Dong Su, Yujie Sun, X. Sunney Xie

Research output: Contribution to journalArticlepeer-review


Allostery is well documented for proteins but less recognized for DNA-protein interactions. Here, we report that specific binding of a protein on DNA is substantially stabilized or destabilized by another protein bound nearby. The ternary complex's free energy oscillates as a function of the separation between the two proteins with a periodicity of ∼10 base pairs, the helical pitch of B-form DNA, and a decay length of ∼15 base pairs. The binding affinity of a protein near a DNA hairpin is similarly dependent on their separation, which - together with molecular dynamics simulations - suggests that deformation of the double-helical structure is the origin of DNA allostery. The physiological relevance of this phenomenon is illustrated by its effect on gene expression in live bacteria and on a transcription factor's affinity near nucleosomes.

Original languageEnglish (US)
Pages (from-to)816-819
Number of pages4
Issue number6121
StatePublished - Feb 15 2013
Externally publishedYes

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Probing allostery through DNA'. Together they form a unique fingerprint.

Cite this