We show that evolutionarily
conserved histidine kinase signal transduction components [9], [10], [11] can be used to build a synthetic signal transduction system, and we then use this system to link input from computationally re-designed receptors to a plant response.
We deleted the phosphate sensing PAS domain [14] from PhoR and made fusions at both the
conserved DHP domain (Dimerization and
Histidine Phosphotransfer) and the charged region (CR).