The Histone Chaperones SET/TAF‐1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c‐Dependent Manner
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. H...
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Published in | Advanced science Vol. 10; no. 29; pp. e2301859 - n/a |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Germany
John Wiley & Sons, Inc
01.10.2023
John Wiley and Sons Inc Wiley |
Subjects | |
Online Access | Get full text |
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Summary: | 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.
This study focuses on the molecular action of two histone chaperones: SET/template‐activating factor‐Iβ and nucleophosmin 1. It is shown how these chaperones have specificity for fully dismantled nucleosomes, characterized the histone eviction (removal) process, and its modulation by cytochrome c. Overall, it is shown that these chaperones exhibit conserved modes of action mediating nucleosome remodeling despite their structural differences. |
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ISSN: | 2198-3844 2198-3844 |
DOI: | 10.1002/advs.202301859 |