Blue-Light-Activated Histidine Kinases: Two-Component Sensors in Bacteria

  title={Blue-Light-Activated Histidine Kinases: Two-Component Sensors in Bacteria},
  author={Trevor E. Swartz and T. S. Tseng and Marcus A Frederickson and Gast{\'o}n Par{\'i}s and Diego J Comerci and Gireesh Rajashekara and Jung-Gun Kim and Mary Beth Mudgett and Gary A. Splitter and Rodolfo Augusto Ugalde and Fernando A. Goldbaum and Winslow R. Briggs and Roberto A. Bogomolni},
  pages={1090 - 1093}
Histidine kinases, used for environmental sensing by bacterial two-component systems, are involved in regulation of bacterial gene expression, chemotaxis, phototaxis, and virulence. Flavin-containing domains function as light-sensory modules in plant and algal phototropins and in fungal blue-light receptors. We have discovered that the prokaryotes Brucella melitensis, Brucella abortus, Erythrobacter litoralis, and Pseudomonas syringae contain light-activated histidine kinases that bind a flavin… 

Light-activated bacterial LOV-domain histidine kinases.

A photosensory two-component system regulates bacterial cell attachment

The differentiating bacterium, Caulobacter crescentus, contains an operon encoding a two-component signaling system consisting of a LOV-histidine kinase, LovK, and a single-domain response regulator, LovR, which results in a light-independent increase in cell–cell attachment in the lovK–lovR overexpression background.

Dimer Asymmetry and Light Activation Mechanism in Brucella Blue-Light Sensor Histidine Kinase

The full-length crystal structure of a blue light photoreceptor LOV histidine kinase involved in light-dependent virulence modulation in the pathogenic bacterium Brucella abortus is reported, providing mechanistic insights into modular sensory proteins that share a similar modular architecture.

Blue light regulated two-component systems: enzymatic and functional analyses of light-oxygen-voltage (LOV)-histidine kinases and downstream response regulators.

In vitro phosphotransfer profiling and enzymatic studies provide a biochemical foundation for this light-regulated signaling module of sensors, effectors, and regulators that control bacterial responses to environmental conditions.

Function, structure and mechanism of bacterial photosensory LOV proteins

The current state of knowledge about the function of bacterial LOV proteins, the structural basis of Lov domain-mediated signal transduction, and the use of LOV domains as genetically encoded photoswitches in synthetic biology are described.

Biology of Light-Sensing Proteins in Plants and Microorganisms

A wide variety of light-sensing proteins that are found in plants and microorganisms and that provide natural resources for engineering optogenetic tools are briefly reviewed and the significance of channelrhodopsins and photoactivated adenylyl cyclases is emphasized.

A blue light inducible two-component signal transduction system in the plant pathogen Pseudomonas syringae pv. tomato.

The open reading frame PSPTO2896 from the plant pathogen Pseudomonas syringae pv. tomato encodes a protein of 534 amino acids showing all salient features of a blue light-driven two-component system.

Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation

The full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346) is reported and the results of biochemical and biophysical studies that explain how it is activated by light are reported.

Ferrochelatase is a conserved downstream target of the blue light-sensing White collar complex in fungi

It is shown that ferrochelatase is also light-regulated in a white collar-dependent fashion in N. crassa and the zygomycete Phycomyces blakesleeanus, indicating that fer rochelatases is an ancient target of photoregulation in the fungal kingdom.



The bacterial counterparts of plant phototropins.

  • A. Losi
  • Biology
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2004
In the bacterial LOV domains, the majority of the amino acids known to interact with the flavin mononucleotide (FMN) chromophore in phototropin LOVs are conserved, supporting the suggestion of their possible role as blue-light sensors.

The Blue-Light Receptor YtvA Acts in the Environmental Stress Signaling Pathway of Bacillus subtilis

Transcriptional analysis of the ytvA structural gene indicated that it provides the entry point for at least one additional environmental input, mediated by the Spx global regulator of disulfide stress, which support a model in which the large signaling complex serves to integrate multiple environmental signals in order to modulate the general stress response.

Initial characterization of a blue-light sensing, phototropin-related protein from Pseudomonas putida: a paradigm for an extended LOV construct.

It is concluded that the protein segment located C-terminally to the LOV core (analogous to an interdomain linker) is enough to confer to the conserved tryptophan the fluorescence characteristics typical of full-length YtvA.

Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction

  • S. CrossonK. Moffat
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2001
Residues that interact with FMN in the phototropin segment of the chimeric fern photoreceptor (phy3) LOV2 are conserved in LOV domains fromphototropin of other plant species and from three proteins involved in the regulation of circadian rhythms in Arabidopsis and Neurospora, suggesting that these domains exhibit the same overall fold and share a common mechanism for flavin binding and light-induced signaling.

Blue Light Activates the σB-Dependent Stress Response of Bacillus subtilis via YtvA

Activation of the general stress response in B. subtilis is modulated by blue light, and the loss and overproduction of YtvA abolish and enhance the increase in sigma(B)-controlled ctc promoter activity at moderate light intensities.

Phototropin blue-light receptors.

  • J. Christie
  • Biology, Environmental Science
    Annual review of plant biology
  • 2007
The photochemical and biochemical events underlying phototropin activation are summarized in addition to the current knowledge of the molecular mechanisms associated with photoreceptor signaling.

The Photocycle of a Flavin-binding Domain of the Blue Light Photoreceptor Phototropin*

It has been shown that the metastable species is likely a flavin-cysteine (Cys39 thiol) adduct at the flavin C(4a) position, and Titrations of LOV2 using chromophore fluorescence as an indicator suggest that Cys39 exists as a thiolate.

The LOV domain family: photoresponsive signaling modules coupled to diverse output domains.

The properties of the light, oxygen, or voltage (LOV) family of blue-light photoreceptor domains, a subset of the Per-ARNT-Sim (PAS) superfamily, are reviewed and the role of this conserved volume of structure in LOV-regulated processes is discussed.