The Histone Chaperones SET/TAF-1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c-Dependent Manner

Pedro Buzón, Alejandro Velázquez-Cruz, Laura Corrales-Guerrero, Antonio Díaz-Quintana, Irene Díaz-Moreno*, Wouter H. Roos*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

Chromatin homeostasis mediates essential processes in eukaryotes, where histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription. The dynamic nature of these processes, however, has severely impeded their characterization at the molecular level. Here, fluorescence optical tweezers are applied to follow histone chaperone dynamics in real time. The molecular action of SET/template-activating factor-Iβ and nucleophosmin 1—representing the two most common histone chaperone folds—are examined using both nucleosomes and isolated histones. It is shown that these chaperones present binding specificity for fully dismantled nucleosomes and are able to recognize and disrupt non-native histone-DNA interactions. Furthermore, the histone eviction process and its modulation by cytochrome c are scrutinized. This approach shows that despite the different structures of these chaperones, they present conserved modes of action mediating nucleosome remodeling.

Original languageEnglish
Article number2301859
Number of pages12
JournalAdvanced science
Volume10
Issue number29
Early online date7-Aug-2023
DOIs
Publication statusPublished - 17-Oct-2023

Keywords

  • fluorescence microscopy
  • nucleophosmin 1
  • optical tweezers
  • SET/template-activating factor-Iβ
  • single-molecule methods

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