"And we found that SIRT6 interacts with multiple parts of the nucleosome, not only the histone where the acetyl flag is to be modified." "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. According to Tan, the nucleosome is a hundred times larger than typical histone peptides used in these studies and are consequently much more complicated to work with. Previous studies have focused on how sirtuins interact with short segments of histones in isolation, in part because such histone "tail" peptides are much easier to work with in the lab. Understanding how sirtuins interact with the nucleosome to remove this flag could inform future drug discovery efforts." Sirtuins can silence gene activity by removing the acetyl flag from histones packaged into nucleosomes. "This packaging can also contribute signals for turning on or turning off genes: Adding an 'acetyl' chemical flag to the histone packaging material turns on a gene, while removing the acetyl flag turns the gene off. Willaman Professor of Molecular Biology at Penn State and an author of the paper. "In our cells, DNA is not naked like we see it in textbooks it is spooled around proteins called histones within a large complex called the nucleosome," said Song Tan, Verne M. Much effort has focused on the ability of some sirtuins to decrease gene expression by removing a chemical flag from histone proteins. ![]() ![]() Because of these varied roles, pharmaceutical companies are exploring their potential for biomedical applications. ![]() 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. A paper describing the results appears April 14 in the journal Science Advances.
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