Skip to Main content Skip to Navigation
Journal articles

Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.

Abstract : Histone acetyltransferases (HATs) play important roles in gene regulation and DNA repair by influencing the accessibility of chromatin to transcription factors and repair proteins. Here, we show that deletion of Gcn5 leads to telomere dysfunction in mouse and human cells. Biochemical studies reveal that depletion of Gcn5 or ubiquitin-specific protease 22 (Usp22), which is another bona fide component of the Gcn5-containing SAGA complex, increases ubiquitination and turnover of TRF1, a primary component of the telomeric shelterin complex. Inhibition of the proteasome or overexpression of USP22 opposes this effect. The USP22 deubiquitinating module requires association with SAGA complexes for activity, and we find that depletion of Gcn5 compromises this association in mammalian cells. Thus, our results indicate that Gcn5 regulates TRF1 levels through effects on Usp22 activity and SAGA integrity.
Document type :
Journal articles
Complete list of metadata
Contributor : Maité Peney Connect in order to contact the contributor
Submitted on : Tuesday, September 29, 2009 - 4:22:36 PM
Last modification on : Tuesday, January 25, 2022 - 12:08:03 PM

Links full text




Boyko S. Atanassov, yvonne A. Evrard, Asha S. Multani, Zhijing Zhang, László Tora, et al.. Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.. Molecular Cell, Cell Press, 2009, 35 (3), pp.352-64. ⟨10.1016/j.molcel.2009.06.015⟩. ⟨inserm-00420788⟩



Record views