Cooperative behavior in the binding of ligands to a protein is often viewed as a complex phenomenon where conformational changes induced by the binding of the ﬁrst ligand leads to tighter binding of subsequent ligands. We revisit the ligand-dependent activation of dimeric transcription factors and show that this process may appear cooperative even when it results from independent ligand binding events. This effect is further accentuated through binding of the activated transcription factor to its cognate operator site on the DNA, where we demonstrate that cooperative activation is a stable ﬁxed point. Our analysis nicely accounts for the apparent cooperativity inherent in the biological activity of many dimeric transcription factors.
Welch, M., Brasen, J. C., Workman, C., & Sams, T. (2020). Origin of cooperativity in the activation of dimeric transcription factors. Physical Review Research, 2(1), . https://doi.org/10.1103/PhysRevResearch.2.013151