2-billion-year-old enzyme reconstructed: Detective work by molecular biologists and bioinformatics researchers

There is a puzzle in the evolution ofbacteria. They were able to explain a hitherto puzzling property of modern enzymes by reconstructing a candidate for a specialRNA polymerase as it existed 2 billion years ago.

They are more effective than their ancestors because they don't work continuously. The reconstruction of the protein from prehistoric times was made possible thanks to the cooperation between the two departments.

The results of the research have been published. There are three building blocks in the sequence C-C-A that are attached to smallRNAs in the cell so that they can later be used to synthesise amolecules.

A team of researchers led by Professor Mrl and Professor Prohaska reconstructed a candidate for an ancestralidase as it existed inbacteria about 2 billion years ago. The research team compared the properties of the reconstructedRNA polymerase with those of the modernbacteria.

Bothidases work with the same precision, but have different reactions. It was not possible to recognize the tendency of modern enzymes to interrupt their activity multiple times. For a long time, this phenomenon puzzled biochemists. The mystery has been solved thanks to the mode of activity of the reconstructedidase.

The ancestralidase works without interruption, but every now and again it removes building blocks that have been correctly added. The results show that a lot can be learned about the evolution and properties of modern enzymes from reconstructing them, and that many questions can only be solved through interaction between the two.

By tracing relationships, you can shimmy into the past.

Gene sequence can be used to create evolutionary trees. The evolutionary path of individual genes can be traced back to a common origin from the diversity of organisms in a tree.

The three step process is what the reconstruction is all about. To be able to look at the sequence of the building blocks, databases have to be searched for corresponding modern enzymes. What the original sequence should have looked like can be calculated using the sequence obtained. The corresponding Gene sequence coding for the old enzyme is introduced into the laboratorybacteria so that they can form the desiredProtein It is possible to study the enzyme in detail to determine its properties.

The breakthrough was when the news came back from the lab that the reconstructed enzyme performs the C-C-A addition even in a wider temperature range than today's enzymes.

Pauses in activity help maximize efficiency.

Evolutionaryly, the enzymes are also improved. Catalysis can run faster and stronger if it's done by anidase. The reconstructed ancestral is able to attach the three C-C-A nucleotides without letting go.

The modern nucleotidyltransferases work in stages with pauses during which they release their substrates. They are more efficient and quicker than their ancestors. The researchers weren't sure what to make of this. Why do modernidases let go of their food?

The reverse reaction in which the incorporated nucleotides are removed again is the reason for the explanation. The reverse reaction in modern Enzymes is almost completely prevented by letting go of the Substrate. They are able to work more efficiently.

Mario Mrl says that they have finally been able to explain why the tRNAs work so well. We were completely surprised by the find. We didn't think this would happen to us. The question was posed 20 years ago and now we can answer it. The close cooperation between the two sciences has existed in Leipzig for several years and has proved to be a great advantage for both sides.

The Substrate affinity versus catalytic efficiency: Ancestral sequence reconstruction of tRNA nucleotidyltransferases solved an enzymes puzzle. There is a book titled "molbev/msac250."

Journal information: Molecular Biology and Evolution

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