AI Article Synopsis
- Histone H2B deubiquitination, primarily done by Ubp8, is normally linked to the SAGA complex, but this study shows that a DUBm can assemble independently of some SAGA components.
- In experiments, cells lacking the SAGA component SPT7 demonstrated reduced recruitment of Ubp8 and Sus1 to genes and chromatin, indicating the importance of SAGA subunits for Ubp8's location and function.
- The findings reveal that while the DUBm can form without all SAGA components, SAGA-CORE subunits still play a crucial role in regulating Ubp8's activity and association with chromatin.
Article Abstract
Background: Histone H2B deubiquitination is performed by numerous deubiquitinases in eukaryotic cells including Ubp8, the catalytic subunit of the tetrameric deubiquitination module (DUBm: Ubp8; Sus1; Sgf11; Sgf73) of the Spt-Ada-Gcn5 acetyltransferase (SAGA). Ubp8 is linked to the rest of SAGA through Sgf73 and is activated by the adaptors Sus1 and Sgf11. It is unknown if DUBm/Ubp8 might also work in a SAGA-independent manner.
Results: Here we report that a tetrameric DUBm is assembled independently of the SAGA-CORE components SPT7, ADA1 and SPT20. In the absence of SPT7, i.e., independent of the SAGA complex, Ubp8 and Sus1 are poorly recruited to SAGA-dependent genes and to chromatin. Notably, cells lacking Spt7 or Ada1, but not Spt20, show lower levels of nuclear Ubp8 than wild-type cells, suggesting a possible role for SAGA-CORE subunits in Ubp8 localization. Last, deletion of SPT7 leads to defects in Ubp8 deubiquitinase activity in in vivo and in vitro assays.
Conclusions: Collectively, our studies show that the DUBm tetrameric structure can form without a complete intact SAGA-CORE complex and that it includes full-length Sgf73. However, subunits of this SAGA-CORE influence DUBm association with chromatin, its localization and its activity.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7594455 | PMC |
| http://dx.doi.org/10.1186/s13072-020-00367-3 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
H2B oncohistones cause homologous recombination defect and genomic instability through reducing H2B monoubiquitination in Schizosaccharomyces pombe.
J Biol Chem
June 2024
Jiangsu Key Laboratory for Microbes and Functional Genomics, College of Life Sciences, Nanjing Normal University, Nanjing, China; School of Basic Medical Sciences, Fujian Medical University, Fuzhou, China. Electronic address:
Article Synopsis
- Scientists studied special changes in histones called noncanonical oncohistones that can cause tumors.
- They found that some of these changes made the yeast cells sensitive to heat and damaging substances, affecting how they repair DNA.
- By blocking a certain protein's function, they were able to help the yeast cells recover some of their DNA repair abilities.
Post-translational covalent conjugation of ubiquitin onto proteins or ubiquitination is important in nearly all cellular processes. Steady-state ubiquitination of individual proteins is maintained by two countering enzymatic activities: conjugation of ubiquitin by E1, E2 and E3 enzymes and removal by deubiquitinases. Here, we deleted one or more genes encoding deubiquitinases in yeast and evaluated the requirements for ubiquitin conjugation onto a target protein.
View Article and Find Full Text PDFDeubiquitination module is critical for oxidative stress response and biofilm formation in Candida glabrata.
Med Mycol
October 2023
Department of Plant Pathology and Microbiology, National Taiwan University, 10617 Taipei, Taiwan.
Candidiasis is one of the most important fungal diseases and generally refers to diseases of the skin or mucosal tissues caused by Candida species. Candida glabrata is an opportunistic human fungal pathogen. Infection with C.
View Article and Find Full Text PDFStructure-function analysis of histone H2B and PCNA ubiquitination dynamics using deubiquitinase-deficient strains.
Sci Rep
October 2023
Department of Radiation Oncology and Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT, 84112, USA.
Post-translational covalent conjugation of ubiquitin onto proteins or ubiquitination is important in nearly all cellular processes. Steady-state ubiquitination of individual proteins in vivo is maintained by two countering enzymatic activities: conjugation of ubiquitin by E1, E2 and E3 enzymes and removal by deubiquitinases. Here, we deleted one or more genes encoding deubiquitinases in yeast and evaluated the requirements for ubiquitin conjugation onto a target protein.
View Article and Find Full Text PDFRole of yUbp8 in Mitochondria and Hypoxia Entangles the Finding of Human Ortholog Usp22 in the Glioblastoma Pseudo-Palisade Microlayer.
Cells
May 2022
Institute of Molecular Biology and Pathology-CNR, Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy.
KAT Gcn5 and DUB Ubp8 are required for respiration and mitochondria functions in budding yeast, and in this study we show that loss of respiratory activity is acquired over time. Interestingly, we show that absence of Ubp8 allows cells to grow in hypoxic conditions with altered mitophagy. Comparatively, the aggressive glioblastoma (GBM) multiforme tumor shows survival mechanisms able to overcome hypoxia in the brain.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!