Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochromec

descriptionPublicationkeyboard_double_arrow_right Article 27 Jul 2015 Spain English Publisher:Proceedings of the National Academy of SciencesJournal:Proceedings of the National Academy of Sciences, volume 112, pages 9,908-9,913 (issn: 0027-8424, eissn: 1091-6490,

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Authors: González-Arzola, K.; Díaz-Moreno, I.; Cano-González, A.; Díaz-Quintana, A.; Velázquez-Campoy, A.; Moreno-Beltrán, B.; López-Rivas, A.; +2 Authors

doi: 10.1073/pnas.1508040112

pmid: 26216969

pmc: PMC4538685

handle: 11441/68902 , 10261/121575

Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochromec

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Abstract

SignificanceHistone chaperones are key regulators of transcriptional activity in damaged chromatin regions in the DNA damage response. Here we show that cytochromec(Cc) targets the histone chaperone SET/template-activating factor (TAF)-Iβ (SET/TAF-Iβ) in the cell nucleus upon DNA damage, resulting in the blocking of the SET/TAF-Iβ function. Ccis actually translocated into the nuclei of cells treated with specific DNA damage inducers and not upon death-receptor pathway or stress-induced stimuli. Cclocks the domains engaged in histone binding of SET/TAF-Iβ, inhibiting its nucleosome assembly activity. Structural characterization of the complex between Ccand SET/TAF-Iβ provides a valuable template for designing drugs aimed at silencing the oncogenic effect of SET/TAF-Iβ.

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Keywords

Models, Molecular, Magnetic Resonance Spectroscopy, Xenopus, Cytochrome c, Binding, Competitive, Histones, Structure-Activity Relationship, Histone chaperone, Animals, Humans, Histone Chaperones, Cell Nucleus, Cytochromes c, ITC, NMR, Protein Structure, Tertiary, DNA-Binding Proteins, Protein Transport, SET-TAF-Iβ, Camptothecin, DNA Damage, HeLa Cells, Molecular Chaperones, Protein Binding, Transcription Factors

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