Shape readout by the transcription factor ETS1 of its RE’s
Transcription in eukaryotes is under the control oftranscription factors (TFs) binding to specific DNA binding sites. ETS proteinsare a family of general TFs that have a conserved DNA binding domain. The ETS1protein regulates the expression of several genes related to differentiation,cell growth, and cancer development. The ETS1 conserved DNA binding domaincontacts the major groove of the DNA double helix at the 5′-GGA/T-3′ core DNAmotif through its helix-turn-helix. Extensive studies show a direct interactionbetween ETS1 protein and the DNA double helix, but there is no data to show howETS1 can differentiate between its multitude of specific DNA binding sites.This research aims therefore to study the global structural and dynamicproperties of consensus-like ETS1 REs, to assess their role in ETS1/DNA interaction.In addition, this study probed the ability of ETS1 to bend the DNA doublehelix, as there are conflicting studies on this question. Both aims werestudied using the cyclization kinetics of the DNA mini-circles method, a methodknown to be able to quantify global aspects of DNA structure and dynamics in arigorous manner.