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PMID:8370470
| Citation |
Meighen, EA (1993) Bacterial bioluminescence: organization, regulation, and application of the lux genes. FASEB J. 7:1016-22 |
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| Abstract |
Significant advances have been made in the characterization of luciferases and other lux-specific proteins as well as the lux genes from a number of different species of marine and terrestrial luminescent bacteria. A common lux gene organization (luxCDAB..E) modulated by the presence of specific genes involved in regulation and flavin binding and metabolism (luxF-I,L,R,Y) has been found with the luciferase genes (luxAB) flanked by the genes involved in synthesis of its fatty aldehyde substrate (luxCDE). For many species, light intensity per cell is highly dependent on cellular growth resulting in a spectacular autoinduction of luminescence at high cell density. Consequently, the bacterial lux system is of particular interest as it can serve as an excellent model for more general signal transduction systems involved in developmental processes, intercellular communication, and even symbioses. Identification of the lux autoinducers and regulatory proteins of Vibrio harveyi and Vibrio fischeri has provided the biochemical and genetic basis for dissection of the luminescent system. Isolation of the lux genes and the ability to transfer these genes into prokaryotic and eukaryotic organisms have greatly expanded the scope and potential uses of bacterial bioluminescence as a safe, rapid, and sensitive sensor for a wide variety of compounds and metabolic processes. |
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| Keywords |
Aldehyde Oxidoreductases/genetics; Genes, Bacterial; Luciferases/genetics; Luminescent Measurements; Riboflavin/biosynthesis; Signal Transduction; Vibrio/genetics; Vibrio/physiology |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0009231: riboflavin biosynthetic process |
ECO:0000270: |
P |
Fig. 1 are genes with sequences corresponding to riboflavin genes involved in the conversion of 6,7-dimethyl-8-ribityllumazine (lumazine) to riboflavin and the biosynthesis of 3,4-dihydroxy- 2-butanone 4-phosphate and lumazine, respectively. |
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