Penn State researchers have revealed how sirtuin enzymes interact with nucleosomes to regulate aging and metabolic processes. Their findings, using cryo-electron microscopy, may inform drug discovery efforts targeting sirtuins for biomedical applications. New scientific research provides insight
New images of the SIRT6 sirtuin enzyme—which regulates aging and other metabolic processes—help explain how it is able to access genetic material within the cell. This cryo-electron microscopy map shows the enzyme in complex with the nucleosome, a tightly packed complex of DNA and proteins called histones. Credit: Song Tan Lab, Penn State
researchers has produced images of a sirtuin enzyme bound to a nucleosome—a tightly packed complex ofand proteins called histones—showing how the enzyme navigates the nucleosome complex to access both DNA and histone proteins and clarifying how it functions in humans and other animals.Sirtuins are a type of enzyme found in organisms ranging from bacteria to humans that play important roles in aging, sensing DNA damage, and suppressing tumors in various cancers.
“We have visualized a sirtuin enzyme called SIRT6 on its physiologically relevant substrate—the entire nucleosome,” said Jean-Paul Armache, assistant professor of biochemistry and molecular biology at Penn State and an author of the paper. “And we found that SIRT6 interacts with multiple parts of the nucleosome, not only the histone where the acetyl flag is to be modified”
“The arginine anchor is a common paradigm for how many chromatin proteins interact with the nucleosome,” said Tan. “When we mutated the SIRT6 arginine anchor, the activity at the K9 position was severely affected, supporting a critical role for the SIRT6’s arginine anchor. Surprisingly, this mutation also impacted SIRT6’s enzymatic activity at a different position, K56, located much further away.”
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