Mgr. Martin Toul, a member of the Protein Engineering team at International Clinical Research Center of St. Anne’s University Hospital Brno (FNUSA-ICRC), won the poster of the day award at the 45th Congress of the Federation of European Biochemical Societies (FEBS). In addition, he also won the Outstanding poster of FEBS Open Bio Editor prize, which was given to only 4 out of a total of 1285 participants. The poster was titled “Engineering protein dynamics for the understanding of the divergent evolution of the Renilla luciferase” and described research on the role of protein dynamics and their high efficiency to understand the evolution of luciferase in Sea pansy (Renilla reniformis) on a molecular level.
Luciferase is the name of enzymes that allow animals to produce light (bioluminescence). The best-known example of an animal using bioluminescence is a firefly. The light is produced as a result of an oxidation reaction of a luciferin molecule in the presence of the enzyme luciferase. The range of bioluminescence colors is relatively extensive, ranging from blue-violet, found mainly in marine organisms including the sea pansy Renilla, to red, which can be seen on the beaches of California during so-called “red tides.”
Luciferase is beneficial not only for organisms in nature but also for laboratory use. It serves as an imaging technique for processes in living organisms, such as insulin secretion imaging. It can also monitor genes, their expression, or their interaction with other biomolecules. Luciferase is also used to monitor the spreading of labeled viruses or cancer cells. Using dynamics engineering of luciferase, Toul, in collaboration with other colleagues from the research team, constructed a new type of luciferase with a 100 times prolonged bioluminescence compared to the original short flash.
“The result is of great importance wherever the enzyme luciferase is used as a diagnostic system for monitoring gene expression or as an imaging technique. The prolongation of bioluminescence can extend the practical application of luciferase even more and make it more efficient, as the original short flash luminescence was not suitable for long-term monitoring of a stable bioluminescence signal. The newly modified protein makes this possible, “concluded Toul.