The SIRT2 deacetylase regulates autoacetylation of p300.
Autoacetylation of the p300 histone acetyltransferase controls the transition between VP16-mediated chromatin acetylation and preinitiation complex (PIC) assembly. Currently, it is unknown if and how autoacetylated p300 is deacetylated. We found that the NAD(+)-dependent histone deacetylase SIRT2 deacetylates p300 in vitro and in cells. SIRT2 deacetylates lysine residues in the ... catalytic domain of p300 and restores binding of p300 to the PIC. RNAi-mediated depletion or chemical inhibition of SIRT2 in cells results in accumulation of acetylated p300. The altered ac-p300/p300 ratio in SIRT2-depleted cells results in decreased p300 recruitment to an integrated VP16-responsive gene and inhibition of transcription. We conclude that p300 undergoes a dynamic cycle of autoacetylation and deacetylation.
Mesh Terms:
Acetylation, Cell Nucleus, Cytoplasm, Hela Cells, Homeostasis, Humans, Kinetics, Protein Processing, Post-Translational, Recombinant Proteins, Sirtuin 2, Sirtuins, p300-CBP Transcription Factors
Acetylation, Cell Nucleus, Cytoplasm, Hela Cells, Homeostasis, Humans, Kinetics, Protein Processing, Post-Translational, Recombinant Proteins, Sirtuin 2, Sirtuins, p300-CBP Transcription Factors
Mol. Cell
Date: Nov. 07, 2008
PubMed ID: 18995842
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