Origin of cooperativity in the activation of dimeric transcription factors

Martin Welch, Jens Christian Brasen, Christopher Workman, Thomas Sams*

*Corresponding author for this work

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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.
Original languageEnglish
Article number013151
JournalPhysical Review Research
Issue number1
Number of pages8
Publication statusPublished - 2020


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