That’s “topo-eye-SO-merase” (to pronounce it), a classic in design in nature:
Biochemist Joe Deweese explains the topoisomerase molecular machine and answers questions submitted by viewers from around the world. The interview is conducted by Casey Luskin, Associate Director of the Center for Science and Culture at Discovery Institute.
Topoisomerase II is an extremely important enzyme in your cells that is designed to untangle knots and supercoils in DNA strands that arise during replication and transcription. It does this by grabbing two tangled DNA segments, holding one steady while it breaks the other segment in two, and then passing the first segment through the break. The second segment is then reconnected, and the two DNA segments are released, having been successfully untangled. Without topoisomerases, chromosomes would become an impossible mess, making DNA replication, transcription, and cell duplication impossible.
The carefully orchestrated untangling activity of topoisomerase II doesn’t happen by accident. This enzyme is a molecular machine that only works because its amino acid sequence is highly specified to provide a special shape and structure necessary for its function. In other words, topoisomerase enzymes contain high levels of complex and specified information—a hallmark of intelligent design.
Joe Deweese received his BS in Biochemistry from Freed-Hardeman University and his PhD in Biochemistry from Vanderbilt University. For twelve years, he taught in the Department of Pharmaceutical Sciences at Lipscomb University. His teaching included biochemistry, molecular biology, genetics, anticancer pharmacology, and cellular physiology. Deweese is starting a new role in August, 2021 as Professor of Biochemistry and Director of Undergraduate Research at Freed-Hardeman University. His research interests include characterizing the mechanism of anti-cancer agents, especially those that target topoisomerase II. Recent studies from his lab have focused on etoposide metabolites, thiosemicarbazones, and natural product derivatives. Currently, his work is focused on examining the differences between the two versions of topoisomerase II found in humans. He and his wife, Liz, have two children.
Here’s the animation: