Journal Article

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

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

2018

Overview

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.

• Publisher: eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publication,eLife Sciences Publications, Ltd
• Subject: Amino Acid Sequence / Arabidopsis / Arabidopsis - genetics / Arabidopsis - metabolism / Arabidopsis Proteins - metabolism / Arabidopsis thaliana / Biochemistry, Molecular Biology / Biodegradation / Cell differentiation / Deoxyribonucleic acid / DET1 / DNA / epigenome / Gene expression / Genes / Genes, Plant / Genomes / Histone H2B / Histone H2B deubiquitination / Histones - metabolism / Homeostasis / Immunoglobulins / Life Sciences / Light / light signaling / Multiprotein Complexes - metabolism / Mutation / Mutation - genetics / Nuclear Proteins - metabolism / Open Reading Frames - genetics / Peptides - chemistry / photomorphogenesis / Plant Biology / Principal components analysis / Protein Binding / Protein Multimerization / Protein Processing, Post-Translational / Protein Subunits - metabolism / Proteins / Proteolysis / RNA polymerase / Saccharomyces cerevisiae - metabolism / SAGA complex / Structural Biology / Transcription / Transcription factors / Ubiquitin / Ubiquitination