Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.

Boyko Atanassov; Yvonne Evrard; Asha Multani; Zhijing Zhang; László Tora; Didier Devys; Sandy Chang; Sharon Dent

doi:10.1016/j.molcel.2009.06.015

Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.

Boyko Atanassov ^{1, 2, 3} Yvonne Evrard ^{1, 2} Asha Multani ⁴ Zhijing Zhang ^{1, 2, 3} László Tora ⁵ Didier Devys ⁵ Sandy Chang ^{4, 6} Sharon Dent ^{1, 2, 3}

1 Department of Biochemistry and Molecular Biology

2 Program in Genes and Development

3 Center for Cancer Epigenetics

4 Department of Genetics

5 IGBMC - Institut de génétique et biologie moléculaire et cellulaire

6 Department of Hematopathology

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.

Type de document :

Article dans une revue

Molecular Cell, Elsevier, 2009, 35 (3), pp.352-64. 〈10.1016/j.molcel.2009.06.015〉

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http://www.hal.inserm.fr/inserm-00420788
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Soumis le : mardi 29 septembre 2009 - 16:22:36
Dernière modification le : mardi 3 juillet 2018 - 10:00:12

Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.

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Gcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.

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