Dimer asymmetry in signaling of blue light sensor histidine kinases

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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. Bd. 12 (2026) Heft 27 . - eaed8943.
ISSN 2375-2548
DOI: https://doi.org/10.1126/sciadv.aed8943

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Abstract

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.