Protein Degradation of RNA Polymerase II-Association Factor 1(PAF1) Is Controlled by CNOT4 and 26S Proteasome

Sun, Haiyan; Kim, Nari; Hwang, Cheol-Sang; Yoo, Joo‐Yeon

doi:10.1371/journal.pone.0125599

Cited by 14 publications

(16 citation statements)

References 32 publications

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“…The E3 ubiquitin ligase Not4/Mot2 has various functions in protein metabolism. Previous work showed that Mot2 controls protein turnover through ubiquitination and proteasome-dependent degradation to regulate chromatin modification, DNA replication, transcription as well as translation ( Panasenko et al, 2006 ; Laribee et al, 2007 ; Mersman et al, 2009 ; Haworth et al, 2010 ; Cooper et al, 2012 ; Sun et al, 2015 ; Laribee et al, 2015 ; Brönner et al, 2017 ). Other studies revealed roles in the functional integrity of the proteasome ( Panasenko and Collart, 2011 ) and in translational quality control ( Dimitrova et al, 2009 ; Halter et al, 2014 ; Preissler et al, 2015 ).…”

Section: Resultsmentioning

confidence: 99%

Ubiquitination-dependent control of sexual differentiation in fission yeast

Simonetti

Candelli

Léon

et al. 2017

eLife

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In fission yeast, meiosis-specific transcripts are selectively eliminated during vegetative growth by the combined action of the YTH-family RNA-binding protein Mmi1 and the nuclear exosome. Upon nutritional starvation, the master regulator of meiosis Mei2 inactivates Mmi1, thereby allowing expression of the meiotic program. Here, we show that the E3 ubiquitin ligase subunit Not4/Mot2 of the evolutionarily conserved Ccr4-Not complex, which associates with Mmi1, promotes suppression of meiotic transcripts expression in mitotic cells. Our analyses suggest that Mot2 directs ubiquitination of Mei2 to preserve the activity of Mmi1 during vegetative growth. Importantly, Mot2 is not involved in the constitutive pathway of Mei2 turnover, but rather plays a regulatory role to limit its accumulation or inhibit its function. We propose that Mmi1 recruits the Ccr4-Not complex to counteract its own inhibitor Mei2, thereby locking the system in a stable state that ensures the repression of the meiotic program by Mmi1.

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Section: Resultsmentioning

confidence: 99%

Ubiquitination-dependent control of sexual differentiation in fission yeast

Simonetti

Candelli

Léon

et al. 2017

eLife

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“…Post-translational modifications of histones such as acetylation, phosphorylation, methylation, ubiquitylation and SUMOylation can affect the properties of chromatin to enhance or suppress gene transcription (36). The ubiquitin-proteasome pathway has been suggested to be involved in elongation phase of transcription to chromatin remodeling/modification; (37) and also in protein degradation of unbound RNA polymerase II associated factor (38). Therefore, downregulation of proteasome's proteases can have a profound effect on gene expression via histone modification, chromatin remodeling and RNA polymerase II associated factor.…”

Section: Discussionmentioning

confidence: 99%

Of Mice and Men

Silswal

Reis

Qureshi

et al. 2017

Shock

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The molecular basis responsible for tolerance following inflammatory response to LPS is not well-understood. We hypothesized that inflammation/tolerance in monocytes/ macrophages is dependent on the proteases of proteasome. To test our hypothesis, first, we examined the expression of different proteasome subunits in different human and mouse monocytes/macrophages. Secondly, we investigated the effect of proteasome subunits/ proteases on LPS-induced expression of tumor necrosis factor-α (TNF-α) and nitric oxide (NO) during inflammation and tolerance using mouse RAW 264.7 macrophages, THP1 cells, and cluster of differentiation 14 positive (CD14+) human monocytes. We found that RAW 264.7 cells (XYZ), mouse peritoneal resident, thioglycollate-elicited macrophages, primed RAW 264.7 (XYZ, LMP) and human monocytes (LMP) expressed different types of proteasome subunits/activities. Cells containing predominantly either LMP subunits (such as THP-1 and human monocytes), or only X, Y, Z subunits (RAW 264.7 cells not primed) could only induce TNF-α, but not NO, while cells containing all five-six subunits (XYZ, LMP) of the proteasome could induce both mediators in response to LPS. Distinct states of inflammation/tolerance in LPS treated cells, strongly correlated with an upregulation or downregulation of proteasome's subunits (proteases), respectively. Moreover, interferon-γ (IFN-γ) treatment of tolerant cells caused robust induction of proteasome's subunit expression in mouse macrophages and human monocytes, and cells regained their ability to respond to LPS. These studies are vital for understanding function of proteasome's subunits during inflammation/tolerance in mouse and human cells, and for design of therapeutic strategies for all diseases based on inflammation.

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“…Not4 appears to contribute to different aspects of transcription from initiation to elongation. It indirectly controls histone H3K4 tri-methylation, an active marker of transcription, by two mechanisms: firstly, by regulating the activity of the PAF1 complex (PAF1C), on the one hand, by facilitating the loading of PAF1C on to promoters and, on the other hand, by ubiquitin-dependent proteolysis of PAF1 not bound to chromatin through the 26S proteasome [166,206]. Set1-directed methylation of H3K4 depends on the PAF1C-dependent ubiquitylation of H2B [207].…”

Section: The Ccr4-not Complex and Transcriptionmentioning

confidence: 99%

The Regulatory Properties of the Ccr4–Not Complex

Hagkarim

Grand

2020

Cells

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The mammalian Ccr4–Not complex, carbon catabolite repression 4 (Ccr4)-negative on TATA-less (Not), is a large, highly conserved, multifunctional assembly of proteins that acts at different cellular levels to regulate gene expression. In the nucleus, it is involved in the regulation of the cell cycle, chromatin modification, activation and inhibition of transcription initiation, control of transcription elongation, RNA export, nuclear RNA surveillance, and DNA damage repair. In the cytoplasm, the Ccr4–Not complex plays a central role in mRNA decay and affects protein quality control. Most of our original knowledge of the Ccr4–Not complex is derived, primarily, from studies in yeast. More recent studies have shown that the mammalian complex has a comparable structure and similar properties. In this review, we summarize the evidence for the multiple roles of both the yeast and mammalian Ccr4–Not complexes, highlighting their similarities.

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Protein Degradation of RNA Polymerase II-Association Factor 1(PAF1) Is Controlled by CNOT4 and 26S Proteasome

Cited by 14 publications

References 32 publications

Ubiquitination-dependent control of sexual differentiation in fission yeast

Ubiquitination-dependent control of sexual differentiation in fission yeast

Of Mice and Men

The Regulatory Properties of the Ccr4–Not Complex

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