2011
DOI: 10.1074/jbc.m111.218990
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Structure and Biochemical Functions of SIRT6

Abstract: SIRT6 is a member of the evolutionarily conserved sirtuin family of NAD ؉ -dependent protein deacetylases and functions in genomic stability and transcriptional control of glucose metabolism. Early reports suggested that SIRT6 performs ADPribosylation, whereas more recent studies have suggested that SIRT6 functions mainly as a histone deacetylase. Thus, the molecular functions of SIRT6 remain uncertain. Here, we perform biochemical, kinetic, and structural studies to provide new mechanistic insight into the fu… Show more

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Cited by 261 publications
(343 citation statements)
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“…Expression and Purification of Recombinant SIRT1-SIRT7-His-tagged SIRT1-7 were overexpressed in BL21(DE3) or BL21(DE3) ⌬CobB Escherichia coli strains and purified as described (19,20).…”
Section: Methodsmentioning
confidence: 99%
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“…Expression and Purification of Recombinant SIRT1-SIRT7-His-tagged SIRT1-7 were overexpressed in BL21(DE3) or BL21(DE3) ⌬CobB Escherichia coli strains and purified as described (19,20).…”
Section: Methodsmentioning
confidence: 99%
“…However, several prior studies indicated that SIRT6 acted through deacetylation of histone marks H3K9Ac (14) and H3K56Ac (15), which modulated HIF1-␣-dependent (16), NF-B-dependent (17), and c-Myc-dependent (3) pathways. In cells, the ability of SIRT6 to promote deacetylation of histones and non-histone proteins (18) seemed at odds with the low in vitro deacetylation rates (13,19) and with the recently described demyristoylation activity (13). X-ray structural analysis of SIRT6 suggested that the low deacetylase activity stems from a splayed configuration between the Rossmann fold domain and the zinc binding subdomain (19).…”
mentioning
confidence: 99%
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“…A homology model for human Sirt1 residues 214-497 (UniProt entry Q96EB6) was generated with Modeller 55 based on an alignment with human Sirt2-34-356 (PDB entry 3ZGO 56 ). Crystal structures of Sirt2 56 , Sirt5 (PDB ID 2B4Y) 57 and Sirt6 (3K35) 58 and the Sirt1 homology model were superimposed on the structure of a Sirt3/peptide complex (3GLR) 59 , and electrostatic potentials were calculated with Adaptive PoissonBoltzmann Solver and mapped on the surface in python molecule viewer 60 .…”
mentioning
confidence: 99%