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Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c
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Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c
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Journal Article
Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c
2015
Overview
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.
Publisher
National Academy of Sciences
Subject
/ Binding, Competitive - drug effects
/ Biophysics and Computational Biology
/ Histone Chaperones - antagonists & inhibitors
/ Histone Chaperones - chemistry
/ Histone Chaperones - metabolism
/ Humans
/ Magnetic Resonance Spectroscopy
/ Molecular Chaperones - antagonists & inhibitors
/ Molecular Chaperones - chemistry
/ Molecular Chaperones - metabolism
/ Protein Binding - drug effects
/ Protein Transport - drug effects
/ Structure-Activity Relationship
/ Transcription Factors - antagonists & inhibitors
/ Transcription Factors - chemistry
/ Transcription Factors - metabolism
/ Xenopus
