Finding the gas pedal on a slow sirtuin

The class III histone deacetylase sirtuin 6 (SIRT6) modulates numerous functions in the cell by deacetylating histone lysine residues. Interestingly, SIRT6's efficiency in in vitro experiments is far greater against substrates carrying long-chain fatty acyl modifications such as myristoylated l...

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Bibliographic Details
Published in:	The Journal of biological chemistry 2020-01, Vol.295 (5), p.1400-1401
Main Authors:	Nielsen, Alexander L., Olsen, Christian A.
Format:	Article
Language:	eng
Subjects:	Catalysis - drug effects Fatty Acids Histone Deacetylases - chemistry Histone Deacetylases - metabolism Histones - metabolism Hydrophobic and Hydrophilic Interactions Kinetics Lysine - metabolism Sirtuins - chemistry Sirtuins - metabolism
Online Access:	Get full text
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Summary:	The class III histone deacetylase sirtuin 6 (SIRT6) modulates numerous functions in the cell by deacetylating histone lysine residues. Interestingly, SIRT6's efficiency in in vitro experiments is far greater against substrates carrying long-chain fatty acyl modifications such as myristoylated lysine compared with acetylated counterparts, but the deacetylase activity can be stimulated by fatty acids and small-molecule allosteric modulators. A new study helps to explain this puzzling activation using a novel activator, thorough kinetic investigation, and mutagenesis studies. These data help elucidate the molecular requirements for activation of SIRT6 and provide a foundation for development of activators for therapeutic purposes.
ISSN:	0021-9258 1083-351X