Olsson O, Koncz C, Szalay A A
Department of Plant Physiology, University of Umeå, Sweden.
Mol Gen Genet. 1988 Dec;215(1):1-9. doi: 10.1007/BF00331295.
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.
