Experimental evidence of a new mechanism of activation of bacterial histidine kinases

Abstract

This data set shows a new mechanism of activation of histidine kinases that participate in signal transduction in bacteria. Experimental evidence was obtained after sequence homology analysis, generation of variant kinases, and their biochemical and structural studies. The techniques used included: construction of modified of the two kinases under study, DesK and EnvZ; transcriptional activation measurements by beta-galactosidase assays, bacterial membrane purification and subsequent, western blot, structural modeling, protein purification and autophosphorylation measurements with radioactively labeled ATP. Value of the data: Histidine kinases are widely distributed in bacteria and play a central role in two-component systems. These are fundamental for the functioning of cells since they are the key to activate and/or inhibit primordial mechanisms by detecting environmental signals and responding adaptively. The mechanism by which this is possible has been established and accepted. In particular, this set of data enables a new perspective on the activation of these systems and can be used to compare with other bacterial kinases already described.