Histone chaperones exhibit conserved functionality in nucleosome remodeling

Chromatin homeostasis mediates some of the most fundamental processes in the eukaryotic cell. In this regard, histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription. However, the dynamic nature of these processes has severely impeded their chara...

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Bibliographic Details
Published inbioRxiv
Main Authors Buzon, Pedro, Velazquez-Cruz, Alejandro, Gonzalez-Arzola, Katiuska, Diaz-Quintana, Antonio, Diaz-Moreno, Irene, Roos, Wouter H
Format Paper
LanguageEnglish
Published Cold Spring Harbor Cold Spring Harbor Laboratory Press 13.01.2022
Subjects
Chaperones
Chromatin remodeling
Cytochrome c
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA repair
Histones
Homeostasis
Nucleosomes
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Summary:Chromatin homeostasis mediates some of the most fundamental processes in the eukaryotic cell. In this regard, histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription. However, the dynamic nature of these processes has severely impeded their characterization at the molecular level. Here we apply single-molecule probing by fluorescence optical tweezers 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, were examined using both nucleosomes and isolated core histones. We show that these chaperones present binding specificity for partially dismantled nucleosomes and are able to recognize and disrupt non-native histone-DNA interactions. Furthermore, we reveal that cytochrome c inhibition of histone chaperones is coupled to chaperone accumulation on DNA-bound histones. Our single-molecule approach shows that despite the drastically different structures of these chaperones, they present conserved modes of action mediating nucleosome remodeling. Competing Interest Statement The authors have declared no competing interest.
DOI:10.1101/2022.01.13.476140