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Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance

ABSTRACT: Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance

PROVIDER: PRJNA486898 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8571270.fastq.gz	Fastqsanger.gz
	SRR8571261.fastq.gz	Fastqsanger.gz
	SRR8571271.fastq.gz	Fastqsanger.gz
	SRR8571262.fastq.gz	Fastqsanger.gz
	SRR8571272.fastq.gz	Fastqsanger.gz

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Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance [RNA-Seq]

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Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance [ChIP-chip]

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Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance [Gene expression]

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Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance [Gene expression]

Project description:Chromatin is a highly regulated environment, and protein association with chromatin is often controlled by post-translational modifications and the corresponding enzymatic machinery. Specifically, SUMO-targeted ubiquitin ligases (STUbLs) have emerged as key players in nuclear quality control, genome maintenance and transcription. However, how STUbLs select specific substrates amongst myriads of SUMOylated proteins on chromatin remains unclear. Here, we reveal a remarkable co-localization of the budding yeast STUbL Slx5/Slx8 and ubiquitin at seven genomic loci that we term ‘ubiquitin hotspots’. Ubiquitylation at these sites depends on Slx5/Slx8 and protein turnover on the Cdc48 segregase. We identify the transcription factor-like Ymr111c/Euc1 to associate with these sites and be a critical determinant of ubiquitylation. Euc1 specifically targets Slx5/Slx8 to ubiquitin hotspots via bipartite binding of Slx5 that involves the Slx5 SUMO-interacting motifs and an additional, novel substrate recognition domain. Interestingly, the Euc1-ubiquitin hotspot pathway acts redundantly with chromatin modifiers of the H2A.Z and Rpd3L pathways in specific stress responses. Thus, our data suggest that STUbL-dependent ubiquitin hotspots shape chromatin during stress adaptation.

2019-03-29 | GSE118817 | GEO

Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance [RNA-Seq]

2019-03-29 | GSE126526 | GEO

Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance [ChIP-chip]

2019-03-29 | GSE118771 | GEO

Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance

Project description:Chromatin is a highly regulated environment, and protein association with chromatin is often controlled by post-translational modifications and the corresponding enzymatic machinery. Specifically, SUMO-targeted ubiquitin ligases (STUbLs) have emerged as key players in nuclear quality control, genome maintenance and transcription. However, how STUbLs select specific substrates amongst myriads of SUMOylated proteins on chromatin remains unclear. Here, we reveal a remarkable co-localization of the budding yeast STUbL Slx5/Slx8 and ubiquitin at seven genomic loci that we term 'ubiquitin hotspots'. Ubiquitylation at these sites depends on Slx5/Slx8 and protein turnover on the Cdc48 segregase. We identify the transcription factor-like Ymr111c/Euc1 to associate with these sites and be a critical determinant of ubiquitylation. Euc1 specifically targets Slx5/Slx8 to ubiquitin hotspots via bipartite binding of Slx5 that involves the Slx5 SUMO-interacting motifs and an additional, novel substrate recognition domain. Interestingly, the Euc1-ubiquitin hotspot pathway acts redundantly with chromatin modifiers of the H2A.Z- and Rpd3L-pathways in specific stress responses. Thus, our data suggest that STUbL-dependent ubiquitin hotspots shape chromatin during stress adaptation.

| S-SCDT-EMBOJ-2018-100368 | biostudies-other

Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance.

Project description:Chromatin is a highly regulated environment, and protein association with chromatin is often controlled by post-translational modifications and the corresponding enzymatic machinery. Specifically, SUMO-targeted ubiquitin ligases (STUbLs) have emerged as key players in nuclear quality control, genome maintenance, and transcription. However, how STUbLs select specific substrates among myriads of SUMOylated proteins on chromatin remains unclear. Here, we reveal a remarkable co-localization of the budding yeast STUbL Slx5/Slx8 and ubiquitin at seven genomic loci that we term "ubiquitin hotspots". Ubiquitylation at these sites depends on Slx5/Slx8 and protein turnover on the Cdc48 segregase. We identify the transcription factor-like Ymr111c/Euc1 to associate with these sites and to be a critical determinant of ubiquitylation. Euc1 specifically targets Slx5/Slx8 to ubiquitin hotspots via bipartite binding of Slx5 that involves the Slx5 SUMO-interacting motifs and an additional, novel substrate recognition domain. Interestingly, the Euc1-ubiquitin hotspot pathway acts redundantly with chromatin modifiers of the H2A.Z and Rpd3L pathways in specific stress responses. Thus, our data suggest that STUbL-dependent ubiquitin hotspots shape chromatin during stress adaptation.

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Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress tolerance

Project description:This SuperSeries is composed of the SubSeries listed below.

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Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders [Saturating mutagenesis]

Project description:Targeted protein degradation is a novel pharmacology established by drugs that recruit target proteins to E3 ubiquitin ligases. Based on the structure of the degrader and the target, different E3 interfaces are critically involved, thus forming defined "functional hotspots". Understanding disruptive mutations in functional hotspots informs on the architecture of the assembly, and highlights residues susceptible to acquire resistance phenotypes. Here, deep mutational scanning revealed hotspots that are conserved or specific for chemically distinct degraders and targets and validated hotspots mutated in patients that relapse from degrader treatment.

2022-09-09 | GSE198278 | GEO

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