Disease relevance of luciferase

• We describe a novel approach to assess toxicity to the free-living nematode Caenorhabditis elegans that relies on the ability of firefly luciferase to report on endogenous ATP levels [1].
• Hybridization studies with the DNA that codes for the two subunits of luciferase revealed considerable homology among all of the strains of X. luminescens and with the DNA of other species of luminous bacteria, but none with the nonluminous Xenorhabdus species [2].

High impact information on luciferase

• The activity of EAAT3 promoter as measured by luciferase reporter activity was increased by RFX1 in C6 cells and the neuron-like SH-SY5Y cells [3].
• Using luciferase assay, we showed that lin-41 expression can be regulated through let-7 complementary sites [4].
• Adenosine triphosphate concentrations were determined by measuring luciferase activity [5].
• Analysis of its promoter region by luciferase reporter assays in transfected HeLa and NIH3T3 cells revealed that an upstream region from -487 to +33 bp of the NLK gene contains significant promoter activity [6].
• This study determined that the bacterial luciferase fusion gene (luxAB) was not a suitable in vivo gene reporter in the model eukaryotic organisms Saccharomyces cerevisiae and Caenorhabditis elegans [7].

Chemical compound and disease context of luciferase

• Toxicity of the bacterial luciferase substrate, n-decyl aldehyde, to Saccharomyces cerevisiae and Caenorhabditis elegans [7].

Biological context of luciferase

• A 487bp segment surrounding the transcription initiation sites increased expression of a luciferase reporter gene 15-fold in Tera-1 cells and was defined as the core promoter region of human GLI [8].

Anatomical context of luciferase

• Although this region has high luciferase activity in COS-1 cells, it is not sufficient to drive GFP expression in zebrafish embryos [9].

Associations of luciferase with chemical compounds

• LuxAB expressing S. cerevisiae strains displayed distinctive rapid decays in luminescence upon addition of the bacterial luciferase substrate, n-decyl aldehyde, suggesting a toxic response [7].
• As the addition of aldehyde is an integral part of the bacterial luciferase activity assay, our results do not support the use of lux reporter genes for in vivo analyses in these model eukaryotic organisms [7].

References