Let there be Light! insights on the origin of luciferase activity from a mealworm AMP-ligase (protoluciferase)

摘要

Beetle luciferases evolved from AMP-ligases. However, it is unclear how the new luciferase activity evolved from AMPligases. In order to clarify such question, several years ago we started to search for luciferase-like enzymes that could simulate a protoluciferase in non-bioluminescent beetles. We discovered a luciferase-like enzyme in Tenebrio molitor mealworms, which was able to produce weak red chemiluminescence in presence of ATP and D-luciferin[1]. However, the identity of such enzyme remained unknown for long time. Recently we cloned one this luciferase-like enzymes from the Malpighi tubules of the closely related Zophobas morio giant mealworm (Fig. 1)[2]. This enzyme is a short AMP-ligase (528 residues), which display a weak luciferase activity in the red region of the spectrum (610 nm), being the fi rst functional protoluciferase model cloned to investigate the origin of luciferase activity.