Molecular biologists and bioinformatics researchers conducted detective work in order to accomplish this feat. The research team, led by Professors Mario Mörl and Sonja Prohaska, focused on enzymes called tRNA nucleotidyltransferases, which attach three nucleotide building blocks in the sequence C
The research team reconstructed an ancestral enzyme by searching databases for corresponding modern enzymes, using the obtained sequences to calculate the original sequence, and introducing the corresponding gene sequence into lab bacteria to produce the desired protein. The enzyme was then studied in detail and compared to modern enzymes.
The research team, led by Professors Mario Mörl and Sonja Prohaska, focused on enzymes called tRNA nucleotidyltransferases, which attach three nucleotide building blocks in the sequence C-C-A to small RNAs in cells. These RNAs are subsequently used to supplyfor protein synthesis. Using phylogenetic reconstructions, the team reconstructed a candidate for an ancestral enzyme that existed in bacteria around 2 billion years ago and compared it to a modern bacterial enzyme.
The ancestral enzyme is processive, i.e. it works without interruption, but every now and then removes nucleotide building blocks that have already been correctly added. The results show that much can be learned about the evolution and properties of modern enzymes from enzyme reconstructions and that many questions can only be solved through interaction between bioinformatics and biochemistry – in a back-and-forth between computer calculations and laboratory experiments.
The reconstruction is essentially a three-step process. First, databases are searched for corresponding modern enzymes in order to be able to examine the sequence of aminobuilding blocks. The sequences obtained can then be used to calculate what the original sequence should have looked like. The corresponding gene sequence coding for the old enzyme is then introduced into laboratory bacteria so that they form the desired protein.
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