ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 59 citations in OpenAlex.
- Tyrosine 67 Phosphorylation Controls Respiration and Limits the Apoptotic Functions of CytochromeCells · 2025Article
- Evolutionary Pro-To-Thr Mutation in the Intrinsically Disordered Domain of ANP32 Family Members Modulates Their Target Binding Modes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Phosphorylation of cytochrome c at tyrosine 48 finely regulates its binding to the histone chaperone SET/TAF-Iβ in the nucleus.Protein science : a publication of the Protein Society · 2024Article
- CytochromeiScience · 2024Article
- The next decade of SET: from an oncoprotein to beyond.Journal of molecular cell biology · 2024Review
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Phosphorylations and Acetylations of CytochromeCells · 2024Review
- The Histone Chaperones SET/TAF-1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c-Dependent Manner.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Article
- Mitochondrial Factors in the Cell Nucleus.International journal of molecular sciences · 2023Review
- Oncoprotein SET dynamically regulates cellular stress response through nucleocytoplasmic transport in breast cancer.Cell biology and toxicology · 2023Article
- De novo sequencing and construction of a unique antibody for the recognition of alternative conformations of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Phosphorylation disrupts long-distance electron transport in cytochrome c.Nature communications · 2022Article
- Nucleus-translocated mitochondrial cytochrome c liberates nucleophosmin-sequestered ARF tumor suppressor by changing nucleolar liquid-liquid phase separation.Nature structural & molecular biology · 2022Article
- Lysosomes: multifunctional compartments ruled by a complex regulatory network.FEBS open bio · 2022Review
- PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022Article
- Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants.FEBS open bio · 2021Article
- Decreased proteasomal cleavage at nitrotyrosine sites in proteins and peptides.Redox biology · 2021Article
- Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus.FEBS open bio · 2021Review
- How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing.Molecules (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chromatin is pivotal for regulation of the DNA damage process insofar as it influences access to DNA and serves as a DNA repair docking site. Recent works identify histone chaperones as key regulators of damaged chromatin's transcriptional activity. However, understanding how chaperones are modulated during DNA damage response is still challenging. This study reveals that the histone chaperone SET/TAF-Iβ interacts with cytochrome c following DNA damage. Specifically, cytochrome c is shown to be translocated into cell nuclei upon induction of DNA damage, but not upon stimulation of the death receptor or stress-induced pathways. Cytochrome c was found to competitively hinder binding of SET/TAF-Iβ to core histones, thereby locking its histone-binding domains and inhibiting its nucleosome assembly activity. In addition, we have used NMR spectroscopy, calorimetry, mutagenesis, and molecular docking to provide an insight into the structural features of the formation of the complex between cytochrome c and SET/TAF-Iβ. Overall, these findings establish a framework for understanding the molecular basis of cytochrome c-mediated blocking of SET/TAF-Iβ, which subsequently may facilitate the development of new drugs to silence the oncogenic effect of SET/TAF-Iβ's histone chaperone activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.