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

Autor: Bianca Habermann, Roman Prytuliak, Markus Höpfler, Stefan Jentsch, Boris Pfander, Tobias Straub, Maximilian J. Kern
Přispěvatelé: Max Planck Institute of Biochemistry (MPIB), Max-Planck-Gesellschaft, Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Collège de France (CdF (institution))-Centre National de la Recherche Scientifique (CNRS), Max-Planck-Institut für Biochemie = Max Planck Institute of Biochemistry (MPIB)
Jazyk: angličtina
Rok vydání: 2019
Předmět:
[SDV]Life Sciences [q-bio]
Chromatin
Epigenetics
Genomics & Functional Genomics
chromatin remodeling
0302 clinical medicine
Ubiquitin
Transcription (biology)
Cdc48/p97
0303 health sciences
biology
General Neuroscience
Articles
ubiquitin Subject Categories Chromatin
Adaptation
Physiological
Chromatin
Cell biology
Small Ubiquitin-Related Modifier Proteins
Epigenetics
Genome
Fungal
Protein Binding
Protein sumoylation
Saccharomyces cerevisiae Proteins
Ubiquitin-Protein Ligases
Saccharomyces cerevisiae
General Biochemistry
Genetics and Molecular Biology
Chromatin remodeling
Article
03 medical and health sciences
Stress
Physiological
ubiquitin
Proteolysis & Proteomics
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
[INFO]Computer Science [cs]
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Molecular Biology
Transcription factor
030304 developmental biology
Binding Sites
General Immunology and Microbiology
Organisms
Genetically Modified
Ubiquitination
Post-translational Modifications
Proteolysis & Proteomics
Sumoylation
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Molecular biology
biology.organism_classification
Chromatin Assembly and Disassembly
Genomics & Functional Genomics
STUbL
SUMO
Proteolysis
biology.protein
Histone deacetylase
[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]
Protein Processing
Post-Translational
030217 neurology & neurosurgery
Post-translational Modifications
Zdroj: EMBO Journal
EMBO Journal, EMBO Press, 2019, 38 (11), ⟨10.15252/embj.2018100368⟩
The EMBO Journal
EMBO Journal, 2019, 38 (11), ⟨10.15252/embj.2018100368⟩
ISSN: 0261-4189
1460-2075
DOI: 10.15252/embj.2018100368⟩
Popis: International audience; 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 chro-matin 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.
Databáze: OpenAIRE
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