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Acetylation of Sirt2 by p300 attenuates its deacetylase activity

Title
Acetylation of Sirt2 by p300 attenuates its deacetylase activity
Authors
Han Y.Jin Y.-H.Kim Y.-J.Kang B.-Y.Choi H.-J.Kim D.-W.Yeo C.-Y.Lee K.-Y.
Ewha Authors
여창열
SCOPUS Author ID
여창열scopus
Issue Date
2008
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 375, no. 4, pp. 576 - 580
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
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. © 2008 Elsevier Inc. All rights reserved.
DOI
10.1016/j.bbrc.2008.08.042
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자연과학대학 > 생명과학전공 > Journal papers
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