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

(2018) ELIFE. 7.
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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.
Keywords
RNA-POLYMERASE-II, UBIQUITIN-CONJUGATING ENZYMES, FLOWERING-LOCUS-C, HISTONE H2B, GENE-EXPRESSION, MESSENGER-RNA, ARABIDOPSIS-THALIANA, TRANSCRIPT ELONGATION, NUCLEAR ARCHITECTURE, NEGATIVE REGULATOR

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MLA
Nassrallah, Amr, Martin Rougée, Clara Bourbousse, et al. “DET1-mediated Degradation of a SAGA-like Deubiquitination Module Controls H2Bub Homeostasis.” ELIFE 7 (2018): n. pag. Print.
APA
Nassrallah, A., Rougée, M., Bourbousse, C., Drevensek, S., Fonseca, S., Iniesto, E., Ait-Mohamed, O., et al. (2018). DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis. ELIFE, 7.
Chicago author-date
Nassrallah, Amr, Martin Rougée, Clara Bourbousse, Stephanie Drevensek, Sandra Fonseca, Elisa Iniesto, Ouardia Ait-Mohamed, et al. 2018. “DET1-mediated Degradation of a SAGA-like Deubiquitination Module Controls H2Bub Homeostasis.” Elife 7.
Chicago author-date (all authors)
Nassrallah, Amr, 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, Vicente Rubio, and Fredy Barneche. 2018. “DET1-mediated Degradation of a SAGA-like Deubiquitination Module Controls H2Bub Homeostasis.” Elife 7.
Vancouver
1.
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;7.
IEEE
[1]
A. Nassrallah et al., “DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis,” ELIFE, vol. 7, 2018.
@article{8581658,
  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.},
  articleno    = {e37892},
  author       = {Nassrallah, Amr and Rougée, Martin and Bourbousse, Clara and Drevensek, Stephanie and Fonseca, Sandra and Iniesto, Elisa and Ait-Mohamed, Ouardia and Deton-Cabanillas, Anne-Flore and Zabulon, Gerald and Ahmed, Ikhlak and Stroebel, David and Masson, Vanessa and Lombard, Berangere and Eeckhout, Dominique and Gevaert, Kris and Loew, Damarys and Genovesio, Auguste and Breyton, Cecile and De Jaeger, Geert and Bowler, Chris and Rubio, Vicente and Barneche, Fredy},
  issn         = {2050-084X},
  journal      = {ELIFE},
  keywords     = {RNA-POLYMERASE-II,UBIQUITIN-CONJUGATING ENZYMES,FLOWERING-LOCUS-C,HISTONE H2B,GENE-EXPRESSION,MESSENGER-RNA,ARABIDOPSIS-THALIANA,TRANSCRIPT ELONGATION,NUCLEAR ARCHITECTURE,NEGATIVE REGULATOR},
  language     = {eng},
  pages        = {29},
  title        = {DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis},
  url          = {http://dx.doi.org/10.7554/elife.37892},
  volume       = {7},
  year         = {2018},
}

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