Luciferase gene

Baldwin, T. O., et al. (1987). Applications of the cloned bacterial luciferase genes luxA and luxB to the study of transcriptional promoters and terminators. In Schoelmerich, J. (ed.), Biolumin. Chemilumin., Proc. Int. Biolumin. Chemilumin. Symp., 4th, 1986, pp. 373-376. Wiley, Chichester, UK. 

Haygood, M. G., and Cohn, D. H. (1986). Luciferase genes cloned from the unculturable luminous bacteroid symbiont of the Caribbean flashlight fish, Kryptophanaron alfredi. Gene 45 203-209. 

Li, L. (2000). Gonyaulax luciferase gene structure, protein expression, and purification from recombinant sources. Method. Enzymol. 305 249-258. 

Li, L., and Hastings, J. W. (1998). The structure and organization of the luciferase gene in the photosynthetic dinoflagellate Gonyaulax polyedra. Plant Mol. Biol. 36 275-284. 

Lorenz, W. W., et al. (1996). Expression of the Renilla reniformis luciferase gene in mammalian cells./. Biolumin. Chemilumin. 11 31-37. 

Palmer, L. M., and Colwell, R. R. (1991). Detection of luciferase gene sequence in nonluminescent Vibrio cholerae by colony hybridization and polymerase chain reaction. Appl. Environ. Microbiol. 57 1286-1293. 

Rodriguez, J. F., et al. (1988). Expression of the firefly luciferase gene in vaccinia virus a highly sensitive gene marker to follow virus dissemination in tissues of infected animals. Proc. Natl. Acad. Sci. USA 85 1667-1671. 

The oral bacterium Streptococcus mutans, containing the luciferase gene of Pyrophorus plagiophtalatus, was used as rapid assay to estimate the effects of various antimicrobial treatments [93],... 

In the method shown in Figure 9B, a firefly luciferase gene is introduced for sensitive bioluminescent detection of target DNA [5], The luciferase-coding DNA requires no posttranslational modification, and the activity of the luciferase produced can be readily measured in the transcription/translation mixture without prior purification. In this assay system, the digoxigenin-labeled probe is first immobilized to polystyrene wells coated with antidigoxigenin antibody. The target... 

ER-CALUX Estrogen receptor-mediated chemically activated luciferase gene expression... 

Assays can be prepared with a reporter system containing, for example, the hrefly luciferase gene. The reporter cells are coupled to receptor genes. When a ligand binds to the receptor, a luminescent glow can be observed. In this way, the effects of the signaling events are evaluated. 

Figure 1 The principles and variant parameters of lipofection. (i) Preparation of a lipofection reagent cationic liposomes were prepared from cationic lipids and helper (if required), (ii) Formation of positively charged lipoplexes by addition of DNA (e.g., reporter plasmid carrying the firefly luciferase gene) to the cationic liposomes, (iii) Transfection (lipofection) by incubation cells with the preformed lipoplexes. The efficiency of gene transfer (lipofection efficiency) can be determined from reporter gene amount or activity (e.g., luciferase activity). Most of the steps of a lipofection experiment can be varied and optimized (grey spots).

Murk, A.J., Legler, J., Denison, M.S., Giesy, J.P, van de Guchte, J., Brouwer, A. (1996). Chemical-activated luciferase gene expression (CALUX ) A novel in vitro bioassay for Ah receptor active compounds in sediments and pore water. FundAppl Toxicol 33 149—160. 

The successful transfer of recombinant DNA into plants was vividly illustrated by an experiment in which the luciferase gene from fireflies was introduced into the cells of a tobacco plant (Fig. 9-29)—a favorite plant for transformation experiments because its cells are particularly easy to transform with Agrobacterium. The potential of this technology is not limited to the production of glow-in-the-dark plants, of course. The same approach has been used to produce crop plants that are resistant to herbicides, plant viruses, and insect pests (Fig. 9-30). Potential benefits include increased yields and less need for environmentally harmful agricultural chemicals. 

In the laboratory, pure firefly luciferin and luciferase are used to measure minute quantities of ATP by the intensity of the light flash produced. As little as a few picomoles (10 12 mol) of ATP can be measured in this way. An enlightening extension of the studies in luciferase was the cloning of the luciferase gene into tobacco plants. When watered with a solution containing luciferin, the plants glowed in the dark (see Fig. 9-29). 

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