P300-mediated acetylation of TRF2 is required for maintaining functional telomeres

Yoon Ra Her, In Kwon Chung

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)


The human telomeric protein TRF2 is required to protect chromosome ends by facilitating their organization into the protective capping structure. Post-translational modifications of TRF2 such as phosphorylation, ubiquitination, SUMOylation, methylation and poly(ADP-ribosyl)ation have been shown to play important roles in telomere function. Here we show that TRF2 specifically interacts with the histone acetyltransferase p300, and that p300 acetylates the lysine residue at position 293 of TRF2. We also report that p300-mediated acetylation stabilizes the TRF2 protein by inhibiting its ubiquitin-dependent proteolysis and is required for efficient telomere binding of TRF2. Furthermore, overexpression of the acetylation-deficient mutant, K293R, induces DNA-damage response foci at telomeres, thereby leading to induction of impaired cell growth, cellular senescence and altered cell cycle distribution. A small but significant number of metaphase chromosomes show no telomeric signals at chromatid ends, suggesting an aberrant telomere structure. These findings demonstrate that acetylation of TRF2 by p300 plays a crucial role in the maintenance of functional telomeres as well as in the regulation of the telomere-Associated DNAdamage response, thus providing a new route for modulating telomere protection function.

Original languageEnglish
Pages (from-to)2267-2283
Number of pages17
JournalNucleic acids research
Issue number4
Publication statusPublished - 2013 Feb

Bibliographical note

Funding Information:
Funding for open access charge: World Class University Fund from the Korean Ministry of Education, Science, and Technology [R31-2009-000-10086-0 to I.K.C.].

All Science Journal Classification (ASJC) codes

  • Genetics


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