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

@article{Swartz2007BlueLightActivatedHK,
  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},
  journal={Science},
  year={2007},
  volume={317},
  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.

From Plant Infectivity to Growth Patterns: The Role of Blue-Light Sensing in the Prokaryotic World

The phylogenetic tree for archaeal LOV domains that have reached a statistically significant number but have not at all been investigated thus far is presented, for the first time, and signatures are beginning to emerge that allow definition of a bona fide LOV or BLUF domain.

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.
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