PNAS2014-03-21 3:03 PM

通过合成萤光素揭示的在果蝇中的潜在荧光素酶活性 Latent luciferase activity in the fruit fly revealed by a synthetic luciferin

意义 
很少有生物能够在黑暗中发光。最出名的莫过于萤火虫了,当小分子D-荧光素通过萤火虫荧光素酶被氧化时,这种小甲虫就可以散发出黄绿色光。我们在此表明,果蝇体内的同源酶也具有生物发光能力,但只有当给予D-荧光素严格合成类似物时,才能实现生物发光。对不发光昆虫的隐藏荧光素酶活性的发现表明生物发光所需的化学天性比旧有认知更普遍,且新酶活性的演变甚至可受未突变新基底表现的引导。 
Significance
Few organisms are capable of glowing in the dark. Perhaps the best known example is the firefly, a beetle that can emit flashes of yellow-green light when the small molecule D-luciferin is oxidized by the enzyme firefly luciferase. Here we show that a homologous enzyme in fruit flies is also capable of bioluminescence, but only when treated with a rigid synthetic analog of D-luciferin. The discovery of hidden luciferase activity in a nonluminescent insect suggests that the inherent chemistry required for bioluminescence is more common than previously thought, and that the evolution of new enzymatic activities can be directed by the appearance of a new substrate even in the absence of mutation.

摘要 
甲虫萤光素酶被认为演变自表现于所有昆虫中的脂酰辅酶A合成酶。这两类酶与ATP一起激活脂肪酸来形成酰基-腺苷酸中间体,但只有荧光素酶可以激活和氧化D-荧光素来发光。我们在此表明无法将D-荧光素作为底物的果蝇脂酰辅酶A合成酶CG6178能够促成合成荧光素类似物CycLuc2发光。可从纯化蛋白,活果蝇Schneider 2细胞以及转染CG6178的哺乳动物细胞中检测到生物发光。因此,无法发光的果蝇具有生物发光的固有能力,但有且仅有在用外源性分子处理后这种发光能力才能得到体现。该研究结果拓宽了生物发光范围并表明新基板的引入可以揭开休眠的酶活性,该过程与酶的正常功能有着显著差异且无需突变。
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.

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