Abstract

Protein photosensors are versatile tools for studying ligand-regulated allostery and signaling. Fundamental to these processes is the amount of energy that can be provided by a photosensor to control downstream signaling events. Such regulation is exemplified by the phototropins—plant serine/threonine kinases that are activated by blue light via conserved LOV (light, oxygen and voltage) domains. The core photosensor of oat phototropin 1 is a LOV domain that interacts in a light-dependent fashion with an adjacent -helix (J) to control kinase activity. We used solution NMR measurements to quantify the free energy of the LOV domain–J-helix binding equilibrium in the dark and lit states. These data indicate that light shifts this equilibrium by 3.8 kcal mol^-1, thus quantifying the energy available through LOV-J for light-driven allosteric regulation. This study provides insight into the energetics of light sensing by phototropins and benchmark values for engineering photoswitchable systems based on the LOV-J interaction.

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