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- W4379231687 abstract "Sirtuin 6 (SIRT6) is a NAD+ dependent histone H3 deacetylase that is prominently found associated with chromatin, attenuates transcriptionally active promoters and regulates DNA repair, metabolic homeostasis and life-span. Unlike other sirtuins it has low affinity to free histone tail but demonstrates strong binding to nucleosomes. It is poorly understood how SIRT6 docking on nucleosomes stimulates its histone de-acetylation activity. Here we present the structure of human SIRT6 bound to a nucleosome determined by cryogenic electron microscopy. The zinc finger domain of SIRT6 associates tightly with the acidic patch of the nucleosome through multiple arginine anchors. The Rossmann fold domain binds to the terminus of the looser DNA half of the nucleosome, detaching two turns of the DNA from the histone octamer and placing the NAD+ binding pocket close to the DNA exit site. This domain shows flexibility with respect to the fixed zinc finger and moves with, but also relative to, the unwrapped DNA terminus. We apply molecular dynamics simulations of the histone tails in the nucleosome to show that in this mode of interaction the active site of SIRT6 is perfectly poised to catalyze deacetylation of the H3 histone tail and that the partial unwrapping of the DNA allows even lysines close to the H3 core to reach the enzyme." @default.
- W4379231687 created "2023-06-04" @default.
- W4379231687 date "2023-06-02" @default.
- W4379231687 modified "2023-10-03" @default.
- W4379231687 title "Joint Public Review: Binding to nucleosome poises SIRT6 for histone H3 de-acetylation" @default.
- W4379231687 doi "https://doi.org/10.7554/elife.87989.1.sa1" @default.
- W4379231687 hasPublicationYear "2023" @default.
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