Acetylation of Sirt2 by p300 attenuates its deacetylase activity

Younho Han, Yun Hye Jin, Yeon Jin Kim, Bok Yun Kang, Hyun Jin Choi, Dae Won Kim, Chang Yeol Yeo, Kwang Youl Lee

Research output: Contribution to journalArticlepeer-review

72 Scopus citations


Histone deacetylases (HDACs) are subdivided into three classes-HDAC I, HDAC II, and Sir2. Sirt proteins are mammalian members of the Sir2 family of NAD+ (nicotinamide adenine dinucleotide)-dependent protein deacetylases. The balance between acetylation and deacetylation of histone and non-histone proteins, regulated by protein acetyltransferases and deacetylases, affects the expression of genes involved in a variety of cellular processes. In addition, HDAC1 is acetylated and regulated by p300, a transcriptional co-activator with protein acetyltransferase activity, suggesting that protein acetyltransferases and deacetylases they control the activities of each other. Although the regulation of HDAC1 by p300 is well characterized, the relationship between Sir2 homologs and p300 is not understood. Here, we report that p300 interacts with Sirt2, a member of the Sir2 family, and triggers the acetylation and subsequent down-regulation of the deacetylation activity of Sirt2, and that the acetylation of Sirt2 by p300 relieves the inhibitory effect of Sirt2 on the transcriptional activity of p53. These observations demonstrate that p300 can inactivate Sirt2 by acetylation and that p300 may regulate the activity of p53 indirectly through Sirt2 in addition to its direct modification of p53.

Original languageEnglish
Pages (from-to)576-580
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 31 Oct 2008

Bibliographical note

Funding Information:
This work was supported by a grant from the Korea Research Foundation Grant funded by the Korean Government (MOEHRD; KRF-2005-041-E00470) to K.-Y. Lee. Y.-J.K. is supported by the second stage of the Brain Korea 21 Project.


  • Acetylation
  • p300
  • p53
  • Sirt2


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