ArticleBMC biochemistry2009
Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interaction.
Article in BMC biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- 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
- The SET oncoprotein promotes estrogen-induced transcription by facilitating establishment of active chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Thirty years of SET/TAF1β/I2PP2A: from the identification of the biological functions to its implications in cancer and Alzheimer's disease.Bioscience reports · 2022Review
- PP2A is activated by cytochromeComputational and structural biotechnology journal · 2022Article
- Mitochondrial cytochrome c shot towards histone chaperone condensates in the nucleus.FEBS open bio · 2021Review
- Targeting of SET/I2PP2A oncoprotein inhibits Gli1 transcription revealing a new modulator of Hedgehog signaling.Scientific reports · 2021Article
- Priming chromatin for segregation: functional roles of mitotic histone modifications.Cell cycle (Georgetown, Tex.) · 2020Review
- Review
- The NMR-based characterization of the FTY720-SET complex reveals an alternative mechanism for the attenuation of the inhibitory SET-PP2A interaction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- CDK1-mediated phosphorylation at H2B serine 6 is required for mitotic chromosome segregation.The Journal of cell biology · 2019Article
- Development and identification of Set transgenic mice.Experimental and therapeutic medicine · 2018Article
- Association between SET expression and glioblastoma cell apoptosis and proliferation.Oncology letters · 2016Article
- A NAP-Family Histone Chaperone Functions in Abiotic Stress Response and Adaptation.Plant physiology · 2016Article
- Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Histone chaperones in Arabidopsis and rice: genome-wide identification, phylogeny, architecture and transcriptional regulation.BMC plant biology · 2015Article
- Regulation of PP2A by Sphingolipid Metabolism and Signaling.Frontiers in oncology · 2014Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe assembly of nucleosomes to higher-order chromatin structures is finely tuned by the relative affinities of histones for chaperones and nucleosomal binding sites. The myeloid leukaemia protein SET/TAF-Ibeta belongs to the NAP1 family of histone chaperones and participates in several chromatin-based mechanisms, such as chromatin assembly, nucleosome reorganisation and transcriptional activation. To better understand the histone chaperone function of SET/TAF-Ibeta, we designed several SET/TAF-Ibeta truncations, examined their structural integrity by circular Dichroism and assessed qualitatively and quantitatively the histone binding properties of wild-type protein and mutant forms using GST-pull down experiments and fluorescence spectroscopy-based binding assays.
resultsWild type SET/TAF-Ibeta binds to histones H2B and H3 with Kd values of 2.87 and 0.15 microM, respectively. The preferential binding of SET/TAF-Ibeta to histone H3 is mediated by its central region and the globular part of H3. On the contrary, the acidic C-terminal tail and the amino-terminal dimerisation domain of SET/TAF-Ibeta, as well as the H3 amino-terminal tail, are dispensable for this interaction.
conclusionThis type of analysis allowed us to assess the relative affinities of SET/TAF-Ibeta for different histones and identify the domains of the protein required for effective histone recognition. Our findings are consistent with recent structural studies of SET/TAF-Ibeta and can be valuable to understand the role of SET/TAF-Ibeta in chromatin function.
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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.