The use of the luxA gene of the bacterial luciferase operon as a reporter gene.
Bacterial luciferase can be assayed rapidly and with high sensitivity both in vivo and in vitro. Here we demonstrate that the N-terminal hydrophobic domain of the alpha catalytic subunit of the luciferase enzyme is indispensable for enzyme activity, although N-terminal translational fusions with full luciferase activity can be obtained. Bacterial luciferase is therefore ideally suited as a reporter enzyme for gene fusion experiments. A list of vectors for the convenient use of the luciferase marker genes to monitor gene expression in vivo are presented.
Olsson
O
O
Department of Plant Physiology, University of Umeå, Sweden.
Koncz
C
C
Szalay
A A
AA
D001483:Base Sequence; D002872:Chromosome Deletion; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D005819:Genetic Markers; D005822:Genetic Vectors; D008156:Luciferases / Q000235:genetics*; D008969:Molecular Sequence Data; D009876:Operon; D010957:Plasmids; D014176:Protein Biosynthesis; D011993:Recombinant Fusion Proteins / Q000235:genetics; D014158:Transcription, Genetic
D004269:DNA, Bacterial; D005819:Genetic Markers; D011993:Recombinant Fusion Proteins; D008156:Luciferases