Abstract
The highly conserved Sir2 family of proteins are involved in regulating chromosome stability and cell aging in eukaryotes, as well as gene silencing in both eukaryotes and archea. Sir2 has nicotinamide adenine dinucleotide (NAD + )-dependent deacetylase activity, and its substrates include histones and the tumor suppressor p53. Starai et al. show that the Salmonella enterica acetyl-CoA synthetase is turned off by posttranslational acetylation of a lysine residue in the active site. The Sir2 homolog CobB switches on the activity of acetyl-CoA synthetase by deacetylating this residue. The conservation of these proteins suggests that lysine acetylation is a common regulatory mechanism in prokaryotes and eukaryotes, in the latter case providing a link between the acetylation of histones and the physiological state of the cell. V. J. Starai, I. Celic, R. N. Cole, J. D. Boeke, J. C. Escalante-Semerena, Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298 , 2390-2392 (2002). [Abstract] [Full Text]
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