Latent luciferase activity in the fruit fly revealed by a synthetic luciferin
Biochemistry & Molecular Pharmacology
Department of Biochemistry and Molecular Pharmacology
Biochemistry | Chemistry | Ecology and Evolutionary Biology
Beetle luciferases are thought to have evolved from fatty acyl-CoA synthetases present in all insects. Both classes of enzymes activate fatty acids with ATP to form acyl-adenylate intermediates, but only luciferases can activate and oxidize d-luciferin to emit light. Here we show that the Drosophila fatty acyl-CoA synthetase CG6178, which cannot use d-luciferin as a substrate, is able to catalyze light emission from the synthetic luciferin analog CycLuc2. Bioluminescence can be detected from the purified protein, live Drosophila Schneider 2 cells, and from mammalian cells transfected with CG6178. Thus, the nonluminescent fruit fly possesses an inherent capacity for bioluminescence that is only revealed upon treatment with a xenobiotic molecule. This result expands the scope of bioluminescence and demonstrates that the introduction of a new substrate can unmask latent enzymatic activity that differs significantly from an enzyme's normal function without requiring mutation.
DOI of Published Version
Proc Natl Acad Sci U S A. 2014 Mar 25;111(12):4443-8. doi: 10.1073/pnas.1319300111. Epub 2014 Mar 10. Link to article on publisher's site
chemical biology, enzymatic promiscuity, evolution, firefly luciferase, imaging
Proceedings of the National Academy of Sciences of the United States of America
Mofford, David M.; Reddy, Gadarla Randheer; and Miller, Stephen C., "Latent luciferase activity in the fruit fly revealed by a synthetic luciferin" (2014). GSBS Student Publications. 2047.