Development of a Light-Dependent Protein Histidine Kinase
Phosphorylation plays a critical role in facilitating signal transduction in prokaryotic and eukaryotic organisms. Our study introduces a tool for investigation of signal diffusion in a biochemical regulation network through the design and characterization of a light-stimulated histidine kinase that consists of the LOV domain from YtvA from Bacillus subtilis and the histidine kinase domain Sln1 from Saccharomyces cerevisiae. We show that blue light can be used as a trigger for modulation of the phosphorylation events in this engineered two-component signal transduction pathway in a eukaryotic cell. At the same time, we demonstrate the robustness of LOV domains and their utility for designing fusion proteins for signal transduction that can be triggered with (blue) light, providing a ready toolkit to design blue light dependent two-component signalling pathways.
Key wordsLight-dependent histidine kinase YtvA Sln1 Phosphorylation Two-component regulation system Nuclear shuttling
This work was supported by the Foundation for Fundamental Research on Matter (FOM) through program number 110 (Spatial design of biochemical regulation networks, SPAT), awarded to Prof. Dr. A. M. Dogterom (AMOLF, Amsterdam, The Netherlands).