at Google ScholarTitle data
Arinkin, Vladimir ; Stadler, Andreas M. ; Meier, Stefanie S. M. ; Jaeger, Karl-Erich ; Möglich, Andreas ; Krauß, Ulrich ; Batra-Safferling, Renu:
Dimer asymmetry in signaling of blue light sensor histidine kinases.
In: Science Advances.
Vol. 12
(2026)
Issue 27
.
- eaed8943.
ISSN 2375-2548
DOI: https://doi.org/10.1126/sciadv.aed8943
Project information
| Project title: |
Project's official title Project's id Bakterielle Phytochrome zur bimodalen Kontrolle Cyclischer Nucleotide 267795153 |
|---|---|
| Project financing: |
Deutsche Forschungsgemeinschaft |
Abstract in another language
Photoreceptor sensory histidine kinases (SHKs) couple light absorption to conformational changes regulating two-component signaling. Despite their importance and widespread use in optogenetics, the underlying structural signaling mechanisms remain poorly understood. Here, we engineered dimeric SHKs based on Pseudomonas putida short light-oxygen-voltage (LOV) proteins, determined their crystal structures, and investigated their signaling mechanisms. Regardless of illumination, the structures adopted a light-state like LOV-LOV dimer with symmetric/straight kinase modules. In contrast, small-angle x-ray scattering together with functional assays revealed pronounced light-dependent rearrangements in solution and allowed the assignment of the kinase-ON dark state to an asymmetric/kinked conformation, whereas the light state adopts a symmetric/straight structure. Comparative analyses of natural and engineered SHKs identified conserved motifs linking light-induced LOV domain rotation to kinase activity. The findings highlight the central role of dimer asymmetry and flexibility in SHK signaling, thereby not least informing the engineering of new light-responsive signaling systems.