Ontology highlight
ABSTRACT:
SUBMITTER: Kim S
PROVIDER: S-EPMC3586787 | biostudies-literature | 2013 Feb
REPOSITORIES: biostudies-literature
Kim Sangjin S Broströmer Erik E Xing Dong D Jin Jianshi J Chong Shasha S Ge Hao H Wang Siyuan S Gu Chan C Yang Lijiang L Gao Yi Qin YQ Su Xiao-dong XD Sun Yujie Y Xie X Sunney XS
Science (New York, N.Y.) 20130201 6121
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 simila ...[more]