Reconstructed ancient protein maps how bacterial enzymes evolved distinct functions
Researchers have reconstructed an ancient bacterial enzyme to understand how proteins evolve distinct functions over time. The study, published in Science Advances, focuses on nucleases and how they specialized to process DNA and RNA building blocks.
Why it matters
Understanding protein evolution provides foundational knowledge for synthetic biology, drug development, and biotechnology applications.
edited by Sadie Harley , reviewed by Robert Egan
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Add as preferred source A glimpse into the molecular past: The 3D structure shows the reconstructed ancestor of the diDNases (A1). Using this “revived” protein, the researchers are investigating how different functions have evolved over time. Credit: Holger Sondermann, DESY How do related proteins develop different functions? This is the question investigated by a research team involving Kiel University, DESY and the Center for Structural Systems Biology (CSSB). Led by Holger Sondermann, professor at Kiel University and head of the Structural Microbiology group at DESY, the researchers reconstructed the common ancestor of two bacterial enzymes and produced the long-extinct protein in the laboratory.
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