In recent decades, many of these luminescent proteins have begun to be utilized experimentally. This study's primary focus is the lux operon of Vibrio fischeri. This operon controls a biosynthetic pathway involving the luciferase enzyme, which emits blue light. This molecular tool has wide-ranging applications as a luminescent probe in studies ranging from oncogenes, to metabolic pathways, and even the monitoring of pollutants in certain water systems. However, it has been demonstrated in previous studies that the luciferase from V. fischeri functions no higher than 30 � C.   For this reason, V. fischeri luciferase cannot be used as a probe in biomedical research in cell lines which must be kept above 30 � C. The introduction of molecular chaperone proteins may allow the enzyme to produce light at higher temperatures, and more extreme pH levels. To test this hypothesis, two sets of E. coli were cultured; one set contained the lux operon only, while the other set of cultures will contain both the lux operon and the groESL operon, which codes for the GroES/EL chaperone complex. Each set of cultures will be grown under two different conditions: constant pH and varying temperatures; constant temperature and varying pH levels. The luminescence from each culture will then be measured. If the GroES/EL complex is successful, then luminescence will be visible in cultures grown in temperatures higher than 30� C.The data gathered will also allow for the construction of a model that will have the ability to predict the temperature and pH conditions for optimal luminescence of this system.

Coexpression of GroES/EL complex with <i>Vibrio fischeri lux</i> operon in E. coli

248th National Meeting (2014)

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Coexpression of GroES/EL complex with Vibrio fischeri lux operon in E. coli