Background
The Sir2 family of proteins were first discovered in Saccharomyces cerevisiae. The sirtuins, class III histone deacetylases (HDAC), are NAD+-dependent protein deacetylases and regulate posttranslational acyl modifications in organisms ranging from bacteria to humans (Haigis and Guarente 2006; Nakagawa and Guarente 2011). The seven sirtuin proteins (SIRT1–SIRT7) in mammals have a conserved core NAD+-binding domain and have diverse substrate proteins, intracellular localizations, and cellular functions (Anderson et al. 2014; Nakagawa and Guarente 2011).
Structure
The sirtuin family of proteins shares a conserved catalytic core of approximately 275 amino acids among most organisms. The acetylated peptide and the NAD+ are bound within a cleft that separates a small zinc-binding domain and a large Rossmann-fold domain. Several invariant amino acids are located...
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Acknowledgments
The work was supported (RR) by a grant (R01GM101927) from the National Institutes of Health, Bethesda, MD, USA.
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Chu, X., George, R., Raju, R. (2016). Sirtuin. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101761-1
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DOI: https://doi.org/10.1007/978-1-4614-6438-9_101761-1
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