Publication Date:
2007-08-25
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swartz, Trevor E -- Tseng, Tong-Seung -- Frederickson, Marcus A -- Paris, Gaston -- Comerci, Diego J -- Rajashekara, Gireesh -- Kim, Jung-Gun -- Mudgett, Mary Beth -- Splitter, Gary A -- Ugalde, Rodolfo A -- Goldbaum, Fernando A -- Briggs, Winslow R -- Bogomolni, Roberto A -- 1.U54-AI-057153/AI/NIAID NIH HHS/ -- R01 GM068886/GM/NIGMS NIH HHS/ -- R01-GM068886/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Aug 24;317(5841):1090-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Santa Cruz, Santa Cruz, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17717187" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/metabolism
;
Animals
;
Brucella abortus/*enzymology/growth & development/pathogenicity
;
Brucella melitensis/*enzymology
;
Cell Line
;
Cloning, Molecular
;
Enzyme Activation
;
Flavin Mononucleotide/metabolism
;
*Light
;
Macrophages/*microbiology
;
Mice
;
Molecular Sequence Data
;
Mutation
;
Phosphorylation
;
Photochemistry
;
Protein Kinases/chemistry/genetics/*metabolism
;
Protein Structure, Tertiary
;
Pseudomonas syringae/*enzymology
;
Signal Transduction
;
Sphingomonadaceae/*enzymology
;
Virulence
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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