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

Author:

Swartz Trevor E.12345,Tseng Tong-Seung12345,Frederickson Marcus A.12345,Paris Gastón12345,Comerci Diego J.12345,Rajashekara Gireesh12345,Kim Jung-Gun12345,Mudgett Mary Beth12345,Splitter Gary A.12345,Ugalde Rodolfo A.12345,Goldbaum Fernando A.12345,Briggs Winslow R.12345,Bogomolni Roberto A.12345

Affiliation:

1. Department of Chemistry and Biochemistry, University of California, Santa Cruz, Santa Cruz, CA, USA.

2. Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA, USA.

3. Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas Buenos Aires–Consejo Nacional de Investigaciones Científicas y Técnicas (IIBBA-CONICET), Buenos Aires, Argentina.

4. Department of Animal Health and Biomedical Sciences, University of Wisconsin, Madison, WI, USA.

5. Department of Biological Sciences, Stanford University, Stanford, CA, USA.

Abstract

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 chromophore and undergo photochemistry indicative of cysteinyl-flavin adduct formation. Infection of macrophages by B. abortus was stimulated by light in the wild type but was limited in photochemically inactive and null mutants, indicating that the flavin-containing histidine kinase functions as a photoreceptor regulating B. abortus virulence.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference29 articles.

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