GSBS Student Publications

Title

Latent luciferase activity in the fruit fly revealed by a synthetic luciferin

Student Author(s)

David M. Mofford

GSBS Program

Biochemistry & Molecular Pharmacology

Publication Date

2014-03-25

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Document Type

Article

Disciplines

Biochemistry | Chemistry | Ecology and Evolutionary Biology

Abstract

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.

Keywords

chemical biology, enzymatic promiscuity, evolution, firefly luciferase, imaging

DOI of Published Version

10.1073/pnas.1319300111

Source

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

Journal/Book/Conference Title

Proceedings of the National Academy of Sciences of the United States of America

Related Resources

Link to Article in PubMed

PubMed ID

24616520

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