The Adaptor Protein ENY2 Is a Component of the Deubiquitination Module of the Arabidopsis SAGA Transcriptional Co-activator Complex but not of the TREX-2 Complex

Pfab, Alexander; Bruckmann, Astrid; Nazet, Julian; Merkl, Rainer; Grasser, Klaus D.

doi:10.1016/j.jmb.2018.03.018

Cited by 30 publications

(27 citation statements)

References 72 publications

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“…Our findings rather unveil a control of the DUBm abundance through targeted proteolysis of the SGF11 subunit. Confirming FRET and yeast two-hybrid assays performed by Pfab et al (2018) , we found direct associations of SGF11 with both UBP22 and ENY2, suggesting that SGF11 is centrally positioned in the DUBm. This property is also visualized on the modeled UBP22 DUBm structures of our two respective studies ( Figure 4D ; Pfab et al, 2018 ).…”

Section: Discussionsupporting

confidence: 68%

“…Confirming FRET and yeast two-hybrid assays performed by Pfab et al (2018) , we found direct associations of SGF11 with both UBP22 and ENY2, suggesting that SGF11 is centrally positioned in the DUBm. This property is also visualized on the modeled UBP22 DUBm structures of our two respective studies ( Figure 4D ; Pfab et al, 2018 ). Hence, C3D-mediated proteolytic degradation of SGF11 is expected to efficiently impair the DUBm activity.…”

Section: Discussionsupporting

confidence: 68%

“…Though, at this stage we also cannot exclude that GFP-ENY2 signal in heterochromatic domains might artifactually result from its overexpression, Arabidopsis ENY2 might therefore display another activity independently from SGF11 and UBP22 in Arabidopsis. As further supported by recent FRAP assays ( Pfab et al, 2018 ), ENY2 function potentially differs from its metazoan counterparts that are enriched at the nuclear periphery ( Rodríguez-Navarro et al, 2004 ).…”

Section: Resultsmentioning

confidence: 86%

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

Nassrallah

Rougée

Bourbousse

et al. 2018

eLife

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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.

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Section: Discussionsupporting

confidence: 68%

Section: Discussionsupporting

confidence: 68%

Section: Resultsmentioning

confidence: 86%

See 1 more Smart Citation

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

Nassrallah

Rougée

Bourbousse

et al. 2018

eLife

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“…For cell imaging, roots (5 -10 DAS) and fragments of Arabidopsis leaves (5 DAS) were mounted in H 2 O on objective slides with cover slips. Confocal laser scanning microscopy (CLSM) was performed using a SP8 microscope (Leica) equipped with 40x/1.3 Oil or 63x/1.3 glycerol objectives as previously described (Dürr et al, 2014;Pfab et al, 2018). GFP was excited using an Argon laser at 488 nm and mCherry/propidium iodide were exited using a DPSS laser at 561 nm.…”

Section: Light Microscopy and Frapmentioning

confidence: 99%

Critical Role of Transcript Cleavage in Arabidopsis RNA Polymerase II Transcriptional Elongation

et al. 2020

Self Cite

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Transcript elongation factors associate with elongating RNA polymerase II (RNAPII) to control the efficiency of mRNA synthesis and consequently modulate plant growth and development. Encountering obstacles during transcription such as nucleosomes or particular DNA sequences may cause backtracking and transcriptional arrest of RNAPII. The elongation factor TFIIS stimulates the intrinsic transcript cleavage activity of the polymerase, which is required for efficient rescue of backtracked/arrested RNAPII. A TFIIS mutant variant (TFIISmut) lacks the stimulatory activity to promote RNA cleavage, but instead efficiently inhibits unstimulated transcript cleavage by RNAPII. We could not recover viable Arabidopsis thaliana tfIIs plants constitutively expressing TFIISmut. Induced, transient expression of TFIISmut in tfIIs plants provoked severe growth defects, transcriptomic changes and massive, transcription-related redistribution of elongating RNAPII within transcribed regions towards the transcriptional start site. The predominant site of RNAPII accumulation overlapped with the +1 nucleosome, suggesting that upon inhibition of RNA cleavage activity, RNAPII arrest prevalently occurs at this position. In the presence of TFIISmut, the amount of RNAPII was reduced, which could be reverted by inhibiting the proteasome, indicating proteasomal degradation of arrested RNAPII. Our findings suggest that polymerase backtracking/arrest frequently occurs in plant cells and RNAPII-reactivation is essential for correct transcriptional output and proper growth/development.

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“…Tra1 is a component of the yeast NuA4 complex 50 . In Arabidopsis, TRA1B interacts with SWC4, a component of the predicted NuA4 complex 67 , and both TRA1A and TRA1B are components of the Arabidopsis SAGA acetyltransferase complex 68 . This suggests that various acetyltransferase complexes may be promoting H2A.Z deposition via histone acetylation.…”

Section: Discussionmentioning

confidence: 99%

Arabidopsis SWR1-associated protein methyl-CpG-binding domain 9 is required for histone H2A.Z deposition

Potok

Zhong

et al. 2019

Preprint

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Deposition of the histone variant H2A.Z by the SWI2/SNF2-Related 1 chromatin remodeling complex (SWR1-C) is important for gene regulation in eukaryotes, but the composition of the Arabidopsis SWR1-C has not been thoroughly characterized. Here identify interacting partners of a conserved Arabidopsis SWR1 subunit, ACTIN-RELATED PROTEIN 6 (ARP6). We isolated nine predicted components, and identified additional interactors implicated in histone acetylation and chromatin biology. One of the novel interacting partners, methyl-CpG-binding domain 9 (MBD9), also strongly interacted with the Imitation SWItch (ISWI) chromatin remodeling complex. MBD9 was required for deposition of H2A.Z at a distinct subset of ARP6-dependent loci. MBD9 was preferentially bound to nucleosome-depleted regions at the 5' ends of genes containing high levels of activating histone marks. These data suggest that MBD9 is a SWR1-C interacting protein required for H2A.Z deposition at a subset of actively transcribing genes.

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The Adaptor Protein ENY2 Is a Component of the Deubiquitination Module of the Arabidopsis SAGA Transcriptional Co-activator Complex but not of the TREX-2 Complex

Cited by 30 publications

References 72 publications

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

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

Critical Role of Transcript Cleavage in Arabidopsis RNA Polymerase II Transcriptional Elongation

Arabidopsis SWR1-associated protein methyl-CpG-binding domain 9 is required for histone H2A.Z deposition

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