DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis

Amr Nassrallah, Martin Rougée, Clara Bourbousse, Stephanie Drevensek, Sandra Fonseca, Elisa Iniesto, Ouardia Ait-Mohamed, Anne Flore Deton-Cabanillas, Gerald Zabulon, Ikhlak Ahmed, David Stroebel, Vanessa Masson, Berangere Lombard, Dominique Eeckhout, Kris Gevaert, Damarys Loew, Auguste Genovesio, Cecile Breyton, Geert de Jaeger, Chris Bowler & 2 others Vicente Rubio, Fredy Barneche

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

DE-ETIOLATED 1 (DET1) is an evolutionarily conserved component of the ubiquitination machinery that mediates the destabilization of key regulators of cell differentiation and proliferation in multicellular organisms. In this study, we provide evidence from Arabidopsis that DET1 is essential for the regulation of histone H2B monoubiquitination (H2Bub) over most genes by controlling the stability of a deubiquitination module (DUBm). In contrast with yeast and metazoan DUB modules that are associated with the large SAGA complex, the Arabidopsis DUBm only comprises three proteins (hereafter named SGF11, ENY2 and UBP22) and appears to act independently as a major H2Bub deubiquitinase activity. Our study further unveils that DET1-DDB1-Associated-1 (DDA1) protein interacts with SGF11 in vivo, linking the DET1 complex to light-dependent ubiquitin-mediated proteolytic degradation of the DUBm. Collectively, these findings uncover a signaling path controlling DUBm availability, potentially adjusting H2Bub turnover capacity to the cell transcriptional status.

Original languageEnglish
Article numbere37892
JournaleLife
Volume7
DOIs
Publication statusPublished - 1 Sep 2018

Fingerprint

Arabidopsis
Homeostasis
Degradation
Ubiquitination
Ubiquitin
Histones
Yeast
Machinery
Cell Differentiation
Proteins
Genes
Yeasts
Cell Proliferation
Availability
Light
Deubiquitinating Enzymes

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

Nassrallah, A., Rougée, M., Bourbousse, C., Drevensek, S., Fonseca, S., Iniesto, E., ... Barneche, F. (2018). DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis. eLife, 7, [e37892]. https://doi.org/10.7554/eLife.37892

DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis. / Nassrallah, Amr; Rougée, Martin; Bourbousse, Clara; Drevensek, Stephanie; Fonseca, Sandra; Iniesto, Elisa; Ait-Mohamed, Ouardia; Deton-Cabanillas, Anne Flore; Zabulon, Gerald; Ahmed, Ikhlak; Stroebel, David; Masson, Vanessa; Lombard, Berangere; Eeckhout, Dominique; Gevaert, Kris; Loew, Damarys; Genovesio, Auguste; Breyton, Cecile; de Jaeger, Geert; Bowler, Chris; Rubio, Vicente; Barneche, Fredy.

In: eLife, Vol. 7, e37892, 01.09.2018.

Research output: Contribution to journalArticle

Nassrallah, A, Rougée, M, Bourbousse, C, Drevensek, S, Fonseca, S, Iniesto, E, Ait-Mohamed, O, Deton-Cabanillas, AF, Zabulon, G, Ahmed, I, Stroebel, D, Masson, V, Lombard, B, Eeckhout, D, Gevaert, K, Loew, D, Genovesio, A, Breyton, C, de Jaeger, G, Bowler, C, Rubio, V & Barneche, F 2018, 'DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis', eLife, vol. 7, e37892. https://doi.org/10.7554/eLife.37892
Nassrallah A, Rougée M, Bourbousse C, Drevensek S, Fonseca S, Iniesto E et al. DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis. eLife. 2018 Sep 1;7. e37892. https://doi.org/10.7554/eLife.37892
Nassrallah, Amr ; Rougée, Martin ; Bourbousse, Clara ; Drevensek, Stephanie ; Fonseca, Sandra ; Iniesto, Elisa ; Ait-Mohamed, Ouardia ; Deton-Cabanillas, Anne Flore ; Zabulon, Gerald ; Ahmed, Ikhlak ; Stroebel, David ; Masson, Vanessa ; Lombard, Berangere ; Eeckhout, Dominique ; Gevaert, Kris ; Loew, Damarys ; Genovesio, Auguste ; Breyton, Cecile ; de Jaeger, Geert ; Bowler, Chris ; Rubio, Vicente ; Barneche, Fredy. / DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis. In: eLife. 2018 ; Vol. 7.
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AU - Rubio, Vicente

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