Journal Article

FZJ-2026-02516

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Dimer asymmetry in signaling of blue-light sensor histidine kinases

Krauss, U. (Corresponding author)FZJ* ; Arinkin, V. ; Stadler, A.FZJ* ; Meier, S.UBT* ; Jaeger, K.-E.FZJ* ; Möglich, A.UBT* ; Batra-Safferling, R. (Corresponding author)FZJ*

2026
Assoc. Washington, DC [u.a.]

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Please use a persistent id in citations: doi:10.1126/sciadv.aed8943

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.

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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)
2. Biotechnologie (IBG-1)

Research Program(s):

1. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2026

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