Related Experiment Video
Updated: Jun 26, 2026

Quantification of Bacterial Histidine Kinase Autophosphorylation Using a Nitrocellulose Binding Assay
Published on: January 11, 2017
Design and signaling mechanism of light-regulated histidine kinases
Andreas Möglich1, Rebecca A Ayers, Keith Moffat
1Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637, USA.
Abstract:
Signal transduction proteins are organized into sensor (input) domains that perceive a signal and, in response, regulate the biological activity of effector (output) domains. We reprogrammed the input signal specificity of a normally oxygen-sensitive, light-inert histidine kinase by replacing its chemosensor domain by a light-oxygen-voltage photosensor domain. Illumination of the resultant fusion kinase YF1 reduced net kinase activity by approximately 1000-fold in vitro. YF1 also controls gene expression in a light-dependent manner in vivo. Signals are transmitted from the light-oxygen-voltage sensor domain to the histidine kinase domain via a 40 degrees -60 degrees rotational movement within an alpha-helical coiled-coil linker; light is acting as a rotary switch. These signaling principles are broadly applicable to domains linked by alpha-helices and to chemo- and photosensors. Conserved sequence motifs guide the rational design of light-regulated variants of histidine kinases and other proteins.
More Related Videos
Related Concept Videos
Cell Signaling in Plants
Amplifying Signals via Enzymatic Cascade
The JAK-STAT Signaling Pathway
Activation and Inactivation of G Proteins
G-Protein Gated Ion Channels
Sensory organs,...
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...

