González-Flecha B, Demple B
Department of Molecular and Cellular Toxicology, Harvard School of Public Health, Boston, Massachusetts 02115.
J Bacteriol. 1994 Apr;176(8):2293-9. doi: 10.1128/jb.176.8.2293-2299.1994.
Luciferase genes are widely used as reporters of gene expression because of the high sensitivity of chemiluminescence detection and the possibility of monitoring light production in intact cells. We engineered fusions of the Escherichia coli soxS promoter to the luciferase structural genes (luxAB) from Vibrio harveyi. Since soxS transcription is positively triggered by the activated SoxR protein in response to agents such as paraquat that generate intracellular superoxide, we hoped to use this construct as a sensitive reporter of redox stress agents. Although a soxR+ soxS'::luxAB fusion exhibited a paraquat-inducible synthesis of luciferase, a smaller increase was consistently observed even in the absence of known soxRS inducers. This endogenous induction was soxR dependent and was further characterized by introducing a plasmid carrying the luciferase structural genes without the soxS promoter into a strain carrying a soxS'::lacZ fusion in the bacterial chromosome. These cells exhibited increased beta-galactosidase expression as they grew into mid-log phase. This increase was ascribed to luciferase activity because beta-galactosidase induction was suppressed (but not eliminated) when the substrate n-decanal was present in the medium. The soxS'::luxAB plasmid transformed superoxide dismutase-deficient strains very poorly under aerobic conditions but just as efficiently as a control plasmid under anaerobic conditions. The production of hydrogen peroxide, the dismutation product of superoxide anion, was significantly increased in strains carrying bacterial luciferase and maximal in the absence of n-decanal. Taken collectively, these data point to the generation of significant amounts of intracellular superoxide by bacterial luciferase, the possible mechanism of which is discussed. In addition to providing insights into the role of superoxide in the activation of the SoxR protein, these results suggest caution in the interpretation of experiments using luciferase as a reporter of gene expression.
由于化学发光检测具有高灵敏度以及能够监测完整细胞中的发光情况,荧光素酶基因被广泛用作基因表达的报告基因。我们构建了大肠杆菌soxS启动子与哈维弧菌荧光素酶结构基因(luxAB)的融合体。由于soxS转录是由活化的SoxR蛋白对诸如百草枯等能产生细胞内超氧化物的试剂作出阳性触发的,我们希望将此构建体用作氧化还原应激试剂的灵敏报告基因。尽管soxR+ soxS'::luxAB融合体表现出百草枯诱导的荧光素酶合成,但即使在没有已知soxRS诱导剂的情况下也始终观察到较小的增加。这种内源性诱导依赖于soxR,通过将携带荧光素酶结构基因但没有soxS启动子的质粒导入在细菌染色体中携带soxS'::lacZ融合体的菌株中进一步进行了表征。这些细胞在进入对数中期生长时表现出β-半乳糖苷酶表达增加。这种增加归因于荧光素酶活性,因为当培养基中存在底物正癸醛时,β-半乳糖苷酶的诱导受到抑制(但未消除)。在需氧条件下,soxS'::luxAB质粒对超氧化物歧化酶缺陷菌株的转化效率非常低,但在厌氧条件下与对照质粒的转化效率一样高。携带细菌荧光素酶的菌株中过氧化氢(超氧阴离子的歧化产物)的产生显著增加,且在没有正癸醛的情况下达到最大。综合来看,这些数据表明细菌荧光素酶会产生大量细胞内超氧化物,并对其可能的机制进行了讨论。除了深入了解超氧化物在SoxR蛋白激活中的作用外,这些结果还提示在解释使用荧光素酶作为基因表达报告基因的实验时要谨慎。